Architecture of a channel-forming O-antigen polysaccharide ABC transporter
The crystal structure of a channel-forming O-antigen polysaccharide ABC transporter suggests a novel biopolymer translocation mechanism. Structure of an O-antigen polysaccharide transporter Bacterial cells are decorated with polysaccharides such as O-antigens, which help them to evade the innate imm...
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Published in | Nature (London) Vol. 553; no. 7688; pp. 361 - 365 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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18.01.2018
Nature Publishing Group |
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Abstract | The crystal structure of a channel-forming O-antigen polysaccharide ABC transporter suggests a novel biopolymer translocation mechanism.
Structure of an O-antigen polysaccharide transporter
Bacterial cells are decorated with polysaccharides such as O-antigens, which help them to evade the innate immune responses of the host. In Gram-negative bacteria, these polysaccharides are transported from the cytoplasm to the periplasm before being incorporated into the outer membrane. In this paper, Jochen Zimmer and colleagues report the crystal structure of a bacterial O-antigen polysaccharide transporter. This represents a key structure in bacterial cell envelope biogenesis. Unusually for ATP-binding cassette (ABC) transporters, which usually operate by an alternating access model, the O-antigen transporter in its open state forms a continuous channel which spans the entire membrane. As a result, the authors suggest that the polysaccharides are transported via a processive mechanism whereby they thread through the open channel.
O-antigens are cell surface polysaccharides of many Gram-negative pathogens that aid in escaping innate immune responses
1
. A widespread O-antigen biosynthesis mechanism involves the synthesis of the lipid-anchored polymer on the cytosolic face of the inner membrane, followed by transport to the periplasmic side where it is ligated to the lipid A core to complete a lipopolysaccharide molecule
2
. In this pathway, transport to the periplasm is mediated by an ATP-binding cassette (ABC) transporter, called Wzm–Wzt. Here we present the crystal structure of the Wzm–Wzt homologue from
Aquifex aeolicus
in an open conformation. The transporter forms a transmembrane channel that is sufficiently wide to accommodate a linear polysaccharide. Its nucleotide-binding domain and a periplasmic extension form ‘gate helices’ at the cytosolic and periplasmic membrane interfaces that probably serve as substrate entry and exit points. Site-directed mutagenesis of the gates impairs
in vivo
O-antigen secretion in the
Escherichia coli
prototype. Combined with a closed structure of the isolated nucleotide-binding domains, our structural and functional analyses suggest a processive O-antigen translocation mechanism, which stands in contrast to the classical alternating access mechanism of ABC transporters. |
---|---|
AbstractList | O-antigens are cell surface polysaccharides of many Gram-negative
pathogens that aid in escaping innate immune responses.
1
A widespread O-antigen biosynthesis
mechanism involves the synthesis of the lipid-anchored polymer on the inner
membrane’s (IM’s) cytosolic face, followed by transport to the
periplasmic side where it is ligated to the lipid A core to complete a
lipopolysaccharide (LPS) molecule
2
. The O antigen’s transport to the periplasm is
mediated by an ATP-binding cassette (ABC) transporter, called Wzm/Wzt,
Extended Data Fig. 1
. We present the crystal
structure of the Wzm/Wzt homolog from
Aquifex aeolicus
in an
open conformation. The transporter forms a transmembrane (TM) channel
sufficiently wide to accommodate a linear polysaccharide. It’s
nucleotide binding domain (NBD) and a periplasmic loop form ‘gate
helices’ at the cytosolic and periplasmic membrane interfaces, likely
serving as substrate entry and exit points. Site-directed mutagenesis of the
gates impairs
in vivo
O antigen secretion in the
E.
coli
prototype. Combined with a closed structure of the isolated
NBDs, our structural and functional analyses suggest a processive O antigen
translocation mechanism, which stands in contrast to the classical alternating
access mechanism of ABC transporters. The crystal structure of a channel-forming O-antigen polysaccharide ABC transporter suggests a novel biopolymer translocation mechanism. The crystal structure of a channel-forming O-antigen polysaccharide ABC transporter suggests a novel biopolymer translocation mechanism. Structure of an O-antigen polysaccharide transporter Bacterial cells are decorated with polysaccharides such as O-antigens, which help them to evade the innate immune responses of the host. In Gram-negative bacteria, these polysaccharides are transported from the cytoplasm to the periplasm before being incorporated into the outer membrane. In this paper, Jochen Zimmer and colleagues report the crystal structure of a bacterial O-antigen polysaccharide transporter. This represents a key structure in bacterial cell envelope biogenesis. Unusually for ATP-binding cassette (ABC) transporters, which usually operate by an alternating access model, the O-antigen transporter in its open state forms a continuous channel which spans the entire membrane. As a result, the authors suggest that the polysaccharides are transported via a processive mechanism whereby they thread through the open channel. O-antigens are cell surface polysaccharides of many Gram-negative pathogens that aid in escaping innate immune responses 1 . A widespread O-antigen biosynthesis mechanism involves the synthesis of the lipid-anchored polymer on the cytosolic face of the inner membrane, followed by transport to the periplasmic side where it is ligated to the lipid A core to complete a lipopolysaccharide molecule 2 . In this pathway, transport to the periplasm is mediated by an ATP-binding cassette (ABC) transporter, called Wzm–Wzt. Here we present the crystal structure of the Wzm–Wzt homologue from Aquifex aeolicus in an open conformation. The transporter forms a transmembrane channel that is sufficiently wide to accommodate a linear polysaccharide. Its nucleotide-binding domain and a periplasmic extension form ‘gate helices’ at the cytosolic and periplasmic membrane interfaces that probably serve as substrate entry and exit points. Site-directed mutagenesis of the gates impairs in vivo O-antigen secretion in the Escherichia coli prototype. Combined with a closed structure of the isolated nucleotide-binding domains, our structural and functional analyses suggest a processive O-antigen translocation mechanism, which stands in contrast to the classical alternating access mechanism of ABC transporters. O-antigens are cell surface polysaccharides of many Gram-negative pathogens that aid in escaping innate immune responses. A widespread O-antigen biosynthesis mechanism involves the synthesis of the lipid-anchored polymer on the cytosolic face of the inner membrane, followed by transport to the periplasmic side where it is ligated to the lipid A core to complete a lipopolysaccharide molecule. In this pathway, transport to the periplasm is mediated by an ATP-binding cassette (ABC) transporter, called Wzm-Wzt. Here we present the crystal structure of the Wzm-Wzt homologue from Aquifex aeolicus in an open conformation. The transporter forms a transmembrane channel that is sufficiently wide to accommodate a linear polysaccharide. Its nucleotide-binding domain and a periplasmic extension form 'gate helices' at the cytosolic and periplasmic membrane interfaces that probably serve as substrate entry and exit points. Site-directed mutagenesis of the gates impairs in vivo O-antigen secretion in the Escherichia coli prototype. Combined with a closed structure of the isolated nucleotide-binding domains, our structural and functional analyses suggest a processive O-antigen translocation mechanism, which stands in contrast to the classical alternating access mechanism of ABC transporters. O-antigens are cell surface polysaccharides of many Gramnegative pathogens that aid in escaping innate immune responses. A widespread O-antigen biosynthesis mechanism involves the synthesis of the lipid-anchored polymer on the cytosolic face of the inner membrane, followed by transport to the periplasmic side where it is ligated to the lipid A core to complete a lipopolysaccharide molecule. In this pathway, transport to the periplasm is mediated by an ATP-binding cassette (ABC) transporter, called Wzm-Wzt. Here we present the crystal structure of the Wzm-Wzt homologue from Aquifex aeolicus in an open conformation. The transporter forms a transmembrane channel that is sufficiently wide to accommodate a linear polysaccharide. Its nucleotide-binding domain and a periplasmic extension form 'gate helices' at the cytosolic and periplasmic membrane interfaces that probably serve as substrate entry and exit points. Site-directed mutagenesis of the gates impairs in vivo O-antigen secretion in the Escherichia coli prototype. Combined with a closed structure of the isolated nucleotide-binding domains, our structural and functional analyses suggest a processive O-antigen translocation mechanism, which stands in contrast to the classical alternating access mechanism of ABC transporters. |
Audience | Academic |
Author | Whitfield, Chris Bi, Yunchen Zimmer, Jochen Mann, Evan |
AuthorAffiliation | 1 Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908, USA 2 Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, N1G 2W1, Canada |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29320481$$D View this record in MEDLINE/PubMed https://www.osti.gov/biblio/1464824$$D View this record in Osti.gov |
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Snippet | The crystal structure of a channel-forming O-antigen polysaccharide ABC transporter suggests a novel biopolymer translocation mechanism.
Structure of an... O-antigens are cell surface polysaccharides of many Gram-negative pathogens that aid in escaping innate immune responses. A widespread O-antigen biosynthesis... The crystal structure of a channel-forming O-antigen polysaccharide ABC transporter suggests a novel biopolymer translocation mechanism. O-antigens are cell surface polysaccharides of many Gramnegative pathogens that aid in escaping innate immune responses. A widespread O-antigen biosynthesis... O-antigens are cell surface polysaccharides of many Gram-negative pathogens that aid in escaping innate immune responses. 1 A widespread O-antigen biosynthesis... |
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SubjectTerms | 631/326/421 631/535/1266 631/57/2270 ABC transporter ABC transporters Adenosine triphosphate Antigens Binding Biosynthesis Cell surface Cellulose Chemical properties Chemical synthesis Conformation Crystal structure E coli Health aspects Helices Homology Humanities and Social Sciences Immune response Innate immunity Interfaces Klebsiella pneumoniae letter Lipid A Lipids Lipopolysaccharides multidisciplinary Periplasm Physiological aspects Polymers Polysaccharides Proteins Saccharides Science Site-directed mutagenesis Structure-function relationships Substrates Translocation Transport Transport proteins |
Title | Architecture of a channel-forming O-antigen polysaccharide ABC transporter |
URI | https://link.springer.com/article/10.1038/nature25190 https://www.ncbi.nlm.nih.gov/pubmed/29320481 https://www.proquest.com/docview/1989835429 https://www.osti.gov/biblio/1464824 https://pubmed.ncbi.nlm.nih.gov/PMC5978415 |
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