Structure of a Voltage-Dependent K+ Channel β Subunit

The integral membrane subunits of many voltage-dependent potassium channels are associated with an additional protein known as the β subunit. One function of β subunits is to modify K+ channel gating. We have determined the structure of the conserved core of mammalian β subunits by X-ray crystallogr...

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Published inCell Vol. 97; no. 7; pp. 943 - 952
Main Authors Gulbis, Jacqueline M, Mann, Sabine, MacKinnon, Roderick
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 25.06.1999
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Abstract The integral membrane subunits of many voltage-dependent potassium channels are associated with an additional protein known as the β subunit. One function of β subunits is to modify K+ channel gating. We have determined the structure of the conserved core of mammalian β subunits by X-ray crystallography at 2.8 Å resolution. Like the integral membrane component of K+ channels, β subunits form a four-fold symmetric structure. Each subunit is an oxido-reductase enzyme complete with a nicotinamide cofactor in its active site. Several structural features of the enzyme active site, including its location with respect to the four-fold axis, imply that it may interact directly or indirectly with the K+ channel’s voltage sensor. This structure suggests a mechanism for coupling membrane electrical excitability directly to chemistry of the cell.
AbstractList The integral membrane subunits of many voltage-dependent potassium channels are associated with an additional protein known as the beta subunit. One function of beta subunits is to modify K+ channel gating. We have determined the structure of the conserved core of mammalian beta subunits by X-ray crystallography at 2.8 A resolution. Like the integral membrane component of K+ channels, beta subunits form a four-fold symmetric structure. Each subunit is an oxidoreductase enzyme complete with a nicotinamide co-factor in its active site. Several structural features of the enzyme active site, including its location with respect to the four-fold axis, imply that it may interact directly or indirectly with the K+ channel's voltage sensor. This structure suggests a mechanism for coupling membrane electrical excitability directly to chemistry of the cell.
The integral membrane subunits of many voltage-dependent potassium channels are associated with an additional protein known as the β subunit. One function of β subunits is to modify K+ channel gating. We have determined the structure of the conserved core of mammalian β subunits by X-ray crystallography at 2.8 Å resolution. Like the integral membrane component of K+ channels, β subunits form a four-fold symmetric structure. Each subunit is an oxido-reductase enzyme complete with a nicotinamide cofactor in its active site. Several structural features of the enzyme active site, including its location with respect to the four-fold axis, imply that it may interact directly or indirectly with the K+ channel’s voltage sensor. This structure suggests a mechanism for coupling membrane electrical excitability directly to chemistry of the cell.
Author MacKinnon, Roderick
Gulbis, Jacqueline M
Mann, Sabine
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  surname: Gulbis
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  fullname: MacKinnon, Roderick
  email: mackinn@rockvax.rockefeller.edu
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/10399921$$D View this record in MEDLINE/PubMed
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Snippet The integral membrane subunits of many voltage-dependent potassium channels are associated with an additional protein known as the β subunit. One function of β...
The integral membrane subunits of many voltage-dependent potassium channels are associated with an additional protein known as the beta subunit. One function...
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SubjectTerms Amino Acid Sequence
Animals
Binding Sites
Crystallography, X-Ray
Electric Conductivity
Humans
Models, Molecular
Molecular Sequence Data
Potassium Channels - chemistry
Protein Conformation
Sequence Homology, Amino Acid
Title Structure of a Voltage-Dependent K+ Channel β Subunit
URI https://dx.doi.org/10.1016/S0092-8674(00)80805-3
https://www.ncbi.nlm.nih.gov/pubmed/10399921
https://search.proquest.com/docview/69879422
Volume 97
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