Crystal structures of the psychrophilic α‐amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor
Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea‐water and it is considered as an extreme psychrophile. We have determined the crystal structures of the α‐amylase (AHA) secreted by this bacterium, in its native state to 2.0 Å resolution as well as in complex with Tris to 1.85...
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Published in | Protein science Vol. 7; no. 3; pp. 564 - 572 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Bristol
Cold Spring Harbor Laboratory Press
01.03.1998
Wiley |
Subjects | |
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Abstract | Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea‐water and it is considered as an extreme psychrophile. We have determined the crystal structures of the α‐amylase (AHA) secreted by this bacterium, in its native state to 2.0 Å resolution as well as in complex with Tris to 1.85 Å resolution. The structure of AHA, which is the first experimentally determined three‐dimensional structure of a psychrophilic enzyme, resembles those of other known α‐amylases of various origins with a surprisingly greatest similarity to mammalian α‐amylases. AHA contains a chlorideion which activates the hydrolytic cleavage of substrate α‐l,4‐glycosidic bonds. The chloride binding site is situated ∼5 Å from the active site which is characterized by a triad of acid residues (Asp 174, Glu 200, Asp 264). These are all involved in firm binding of the Tris moiety. A reaction mechanism for substrate hydrolysis is proposed on the basis of the Tris inhibitor binding and the chloride activation.A trio of residues (Ser 303, His 337, Glu 19) having a striking spatial resemblance with serine‐protease like catalytic triads was found ∼22 Å from the active site. We found that this triad is equally present in other chloride dependent α‐amylases, and suggest that it could be responsible for autoproteolytic events observed in solution for this cold adapted α‐amylase. |
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AbstractList | Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea-water and it is considered as an extreme psychrophile. We have determined the crystal structures of the alpha-amylase (AHA) secreted by this bacterium, in its native state to 2.0 angstroms resolution as well as in complex with Tris to 1.85 angstroms resolution. The structure of AHA, which is the first experimentally determined three-dimensional structure of a psychrophilic enzyme, resembles those of other known alpha-amylases of various origins with a surprisingly greatest similarity to mammalian alpha-amylases. AHA contains a chloride ion which activates the hydrolytic cleavage of substrate alpha-1,4-glycosidic bonds. The chloride binding site is situated approximately 5 angstroms from the active site which is characterized by a triad of acid residues (Asp 174, Glu 200, Asp 264). These are all involved in firm binding of the Tris moiety. A reaction mechanism for substrate hydrolysis is proposed on the basis of the Tris inhibitor binding and the chloride activation. A trio of residues (Ser 303, His 337, Glu 19) having a striking spatial resemblance with serine-protease like catalytic triads was found approximately 22 angstroms from the active site. We found that this triad is equally present in other chloride dependent alpha-amylases, and suggest that it could be responsible for autoproteolytic events observed in solution for this cold adapted alpha-amylase. Abstract Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea‐water and it is considered as an extreme psychrophile. We have determined the crystal structures of the α‐amylase (AHA) secreted by this bacterium, in its native state to 2.0 Å resolution as well as in complex with Tris to 1.85 Å resolution. The structure of AHA, which is the first experimentally determined three‐dimensional structure of a psychrophilic enzyme, resembles those of other known α‐amylases of various origins with a surprisingly greatest similarity to mammalian α‐amylases. AHA contains a chlorideion which activates the hydrolytic cleavage of substrate α‐l,4‐glycosidic bonds. The chloride binding site is situated ∼5 Å from the active site which is characterized by a triad of acid residues (Asp 174, Glu 200, Asp 264). These are all involved in firm binding of the Tris moiety. A reaction mechanism for substrate hydrolysis is proposed on the basis of the Tris inhibitor binding and the chloride activation.A trio of residues (Ser 303, His 337, Glu 19) having a striking spatial resemblance with serine‐protease like catalytic triads was found ∼22 Å from the active site. We found that this triad is equally present in other chloride dependent α‐amylases, and suggest that it could be responsible for autoproteolytic events observed in solution for this cold adapted α‐amylase. Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea-water and it is considered as an extreme psychrophile. We have determined the crystal structures of the alpha-amylase (AHA) secreted by this bacterium, in its native state to 2.0 angstroms resolution as well as in complex with Tris to 1.85 angstroms resolution. The structure of AHA, which is the first experimentally determined three-dimensional structure of a psychrophilic enzyme, resembles those of other known alpha-amylases of various origins with a surprisingly greatest similarity to mammalian alpha-amylases. AHA contains a chloride ion which activates the hydrolytic cleavage of substrate alpha-1,4-glycosidic bonds. The chloride binding site is situated approximately 5 angstroms from the active site which is characterized by a triad of acid residues (Asp 174, Glu 200, Asp 264). These are all involved in firm binding of the Tris moiety. A reaction mechanism for substrate hydrolysis is proposed on the basis of the Tris inhibitor binding and the chloride activation. A trio of residues (Ser 303, His 337, Glu 19) having a striking spatial resemblance with serine-protease like catalytic triads was found approximately 22 angstroms from the active site. We found that this triad is equally present in other chloride dependent alpha-amylases, and suggest that it could be responsible for autoproteolytic events observed in solution for this cold adapted alpha-amylase.Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea-water and it is considered as an extreme psychrophile. We have determined the crystal structures of the alpha-amylase (AHA) secreted by this bacterium, in its native state to 2.0 angstroms resolution as well as in complex with Tris to 1.85 angstroms resolution. The structure of AHA, which is the first experimentally determined three-dimensional structure of a psychrophilic enzyme, resembles those of other known alpha-amylases of various origins with a surprisingly greatest similarity to mammalian alpha-amylases. AHA contains a chloride ion which activates the hydrolytic cleavage of substrate alpha-1,4-glycosidic bonds. The chloride binding site is situated approximately 5 angstroms from the active site which is characterized by a triad of acid residues (Asp 174, Glu 200, Asp 264). These are all involved in firm binding of the Tris moiety. A reaction mechanism for substrate hydrolysis is proposed on the basis of the Tris inhibitor binding and the chloride activation. A trio of residues (Ser 303, His 337, Glu 19) having a striking spatial resemblance with serine-protease like catalytic triads was found approximately 22 angstroms from the active site. We found that this triad is equally present in other chloride dependent alpha-amylases, and suggest that it could be responsible for autoproteolytic events observed in solution for this cold adapted alpha-amylase. Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea‐water and it is considered as an extreme psychrophile. We have determined the crystal structures of the α‐amylase (AHA) secreted by this bacterium, in its native state to 2.0 Å resolution as well as in complex with Tris to 1.85 Å resolution. The structure of AHA, which is the first experimentally determined three‐dimensional structure of a psychrophilic enzyme, resembles those of other known α‐amylases of various origins with a surprisingly greatest similarity to mammalian α‐amylases. AHA contains a chlorideion which activates the hydrolytic cleavage of substrate α‐l,4‐glycosidic bonds. The chloride binding site is situated ∼5 Å from the active site which is characterized by a triad of acid residues (Asp 174, Glu 200, Asp 264). These are all involved in firm binding of the Tris moiety. A reaction mechanism for substrate hydrolysis is proposed on the basis of the Tris inhibitor binding and the chloride activation.A trio of residues (Ser 303, His 337, Glu 19) having a striking spatial resemblance with serine‐protease like catalytic triads was found ∼22 Å from the active site. We found that this triad is equally present in other chloride dependent α‐amylases, and suggest that it could be responsible for autoproteolytic events observed in solution for this cold adapted α‐amylase. |
Author | Feller, Georges Aghajari, Nushin Gerday, Charles Haser, Richard |
AuthorAffiliation | Laboratoire d'Architecture et Fonction des Macromolécules Biologiques, UPR9039, Institut de Biologie Structurale et Microbiologie, IFR1, CNRS, Marseille, France |
AuthorAffiliation_xml | – name: Laboratoire d'Architecture et Fonction des Macromolécules Biologiques, UPR9039, Institut de Biologie Structurale et Microbiologie, IFR1, CNRS, Marseille, France |
Author_xml | – sequence: 1 givenname: Nushin surname: Aghajari fullname: Aghajari, Nushin – sequence: 2 givenname: Richard surname: Haser fullname: Haser, Richard email: r.haser@ibcp.fr – sequence: 3 givenname: Georges surname: Feller fullname: Feller, Georges – sequence: 4 givenname: Charles surname: Gerday fullname: Gerday, Charles |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9541387$$D View this record in MEDLINE/PubMed https://hal.science/hal-00313564$$DView record in HAL |
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Snippet | Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea‐water and it is considered as an extreme psychrophile. We have determined the crystal... Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea-water and it is considered as an extreme psychrophile. We have determined the crystal... Abstract Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea‐water and it is considered as an extreme psychrophile. We have determined the... |
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SubjectTerms | allosteric activation Allosteric Regulation alpha-Amylases - antagonists & inhibitors alpha-Amylases - ultrastructure Bacterial Proteins - ultrastructure Binding Sites Biochemistry, Molecular Biology Buffers Calcium Chlorides cold adaptation Cold Temperature crystal structure Crystallography, X-Ray Enzyme Inhibitors - chemistry glycosyl hydrolases Gram-Negative Bacteria - enzymology inhibition Life Sciences Models, Molecular Molecular Sequence Data Protein Structure, Secondary psychrophilic Serine Proteinase Inhibitors |
Title | Crystal structures of the psychrophilic α‐amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor |
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