1x8h: Difference between revisions

Revision as of 15:27, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1x8h.png

Template:STRUCTURE 1x8h

The Mono-Zinc Carbapenemase CphA (N220G mutant) Shows a Zn(II)- NH2 ARG CoordinationThe Mono-Zinc Carbapenemase CphA (N220G mutant) Shows a Zn(II)- NH2 ARG Coordination

Template:ABSTRACT PUBMED 15588826

About this StructureAbout this Structure

1X8H is a Single protein structure of sequence from Aeromonas hydrophila. Full crystallographic information is available from OCA.

ReferenceReference

A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem., Garau G, Bebrone C, Anne C, Galleni M, Frere JM, Dideberg O, J Mol Biol. 2005 Jan 28;345(4):785-95. PMID:15588826

Update of the standard numbering scheme for class B beta-lactamases., Garau G, Garcia-Saez I, Bebrone C, Anne C, Mercuri P, Galleni M, Frere JM, Dideberg O, Antimicrob Agents Chemother. 2004 Jul;48(7):2347-9. PMID:15215079

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold., Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O, EMBO J. 1995 Oct 16;14(20):4914-21. PMID:7588620

Guanidine is a Zn(2+)-binding ligand at neutral pH in aqueous solution., Aoki S, Iwaida K, Hanamoto N, Shiro M, Kimura E, J Am Chem Soc. 2002 May 15;124(19):5256-7. PMID:11996552

Page seeded by OCA on Sun Jul 27 15:27:04 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1x8h.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1x8h|  PDB=1x8h  |  SCENE=  }}
-'''The Mono-Zinc Carbapenemase CphA (N220G mutant) Shows a Zn(II)- NH2 ARG Coordination'''
+===The Mono-Zinc Carbapenemase CphA (N220G mutant) Shows a Zn(II)- NH2 ARG Coordination===
-==Overview==
+<!--
-One strategy developed by bacteria to resist the action of beta-lactam antibiotics is the expression of metallo-beta-lactamases. CphA from Aeromonas hydrophila is a member of a clinically important subclass of metallo-beta-lactamases that have only one zinc ion in their active site and for which no structure is available. The crystal structures of wild-type CphA and its N220G mutant show the structural features of the active site of this enzyme, which is modeled specifically for carbapenem hydrolysis. The structure of CphA after reaction with a carbapenem substrate, biapenem, reveals that the enzyme traps a reaction intermediate in the active site. These three X-ray structures have allowed us to propose how the enzyme recognizes carbapenems and suggest a mechanistic pathway for hydrolysis of the beta-lactam. This will be relevant for the design of metallo-beta-lactamase inhibitors as well as of antibiotics that escape their hydrolytic activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_15588826}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15588826 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15588826}}
 ==About this Structure==
@@ Line 20: / Line 24: @@
 ==Reference==
 A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem., Garau G, Bebrone C, Anne C, Galleni M, Frere JM, Dideberg O, J Mol Biol. 2005 Jan 28;345(4):785-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15588826 15588826]
+Update of the standard numbering scheme for class B beta-lactamases., Garau G, Garcia-Saez I, Bebrone C, Anne C, Mercuri P, Galleni M, Frere JM, Dideberg O, Antimicrob Agents Chemother. 2004 Jul;48(7):2347-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15215079 15215079]
+The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold., Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O, EMBO J. 1995 Oct 16;14(20):4914-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7588620 7588620]
+Guanidine is a Zn(2+)-binding ligand at neutral pH in aqueous solution., Aoki S, Iwaida K, Hanamoto N, Shiro M, Kimura E, J Am Chem Soc. 2002 May 15;124(19):5256-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11996552 11996552]
 [[Category: Aeromonas hydrophila]]
 [[Category: Beta-lactamase]]
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 [[Category: Garau, G.]]
 [[Category: Hydrolase]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:27:04 2008''