2qjs

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{{STRUCTURE_2qjs| PDB=2qjs | SCENE= }}
{{STRUCTURE_2qjs| PDB=2qjs | SCENE= }}
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'''Stenotrophomonas maltophilia L1 metallo-beta-lactamase Asp-120 Asn mutant'''
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===Stenotrophomonas maltophilia L1 metallo-beta-lactamase Asp-120 Asn mutant===
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==Overview==
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Metallo-beta-lactamases (mbetals) are zinc-dependent enzymes that hydrolyze a wide range of beta-lactam antibiotics. The mbetal active site features an invariant Asp-120 that ligates one of the two metal ions (Zn2) and a metal-bridging water/hydroxide (Wat1). Previous studies show that substitutions at Asp-120 dramatically affect mbetal activity, but no consensus exists as to its role in beta-lactam turnover. Here we present crystal structures of the Asn and Cys mutants of Asp-120 of the L1 mbetal from Stenotrophomonas maltophilia. Both mutants retain a dinuclear zinc center with Wat1 present. In the essentially inactive Cys enzyme Zn2 is displaced to a more buried position relative to that in the wild-type enzyme. In the catalytically impaired Asn enzyme the coordination of Zn2 is altered, neither it nor Wat1 is coordinated by Asn-120, and the N-terminal 19 amino acids, important to cooperative interactions between subunits in the wild-type enzyme, are disordered. Comparison with the structure of L1 complexed with the hydrolyzed oxacephem moxalactam suggests that in the Cys mutant Zn2 can no longer make stabilizing interactions with anionic nitrogen species formed in the hydrolytic reaction. The diminished activity of the Asn mutant arises from a combination of loss of intersubunit interactions and impaired proton transfer to, and reduced interaction of Zn2 with, the substrate amide nitrogen. We conclude that, while interactions of Asp-120 with active site water molecules are important to proton transfer and possibly nucleophilic attack by Wat1, its primary role is to optimally position Zn2 for catalytically important interactions with the charged amide nitrogen of substrate.
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The line below this paragraph, {{ABSTRACT_PUBMED_17715946}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 17715946 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17715946}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural basis for the role of Asp-120 in metallo-beta-lactamases., Crisp J, Conners R, Garrity JD, Carenbauer AL, Crowder MW, Spencer J, Biochemistry. 2007 Sep 18;46(37):10664-74. Epub 2007 Aug 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17715946 17715946]
Structural basis for the role of Asp-120 in metallo-beta-lactamases., Crisp J, Conners R, Garrity JD, Carenbauer AL, Crowder MW, Spencer J, Biochemistry. 2007 Sep 18;46(37):10664-74. Epub 2007 Aug 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17715946 17715946]
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Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis., Garrity JD, Carenbauer AL, Herron LR, Crowder MW, J Biol Chem. 2004 Jan 9;279(2):920-7. Epub 2003 Oct 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14573595 14573595]
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Metallo-beta-lactamase]]
[[Category: Metallo-beta-lactamase]]
[[Category: Zinc]]
[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:04:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:47:24 2008''

Revision as of 18:47, 27 July 2008

Image:2qjs.png

Template:STRUCTURE 2qjs

Stenotrophomonas maltophilia L1 metallo-beta-lactamase Asp-120 Asn mutant

Template:ABSTRACT PUBMED 17715946

About this Structure

2QJS is a Single protein structure of sequence from Stenotrophomonas maltophilia. Full crystallographic information is available from OCA.

Reference

Structural basis for the role of Asp-120 in metallo-beta-lactamases., Crisp J, Conners R, Garrity JD, Carenbauer AL, Crowder MW, Spencer J, Biochemistry. 2007 Sep 18;46(37):10664-74. Epub 2007 Aug 23. PMID:17715946

Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis., Garrity JD, Carenbauer AL, Herron LR, Crowder MW, J Biol Chem. 2004 Jan 9;279(2):920-7. Epub 2003 Oct 22. PMID:14573595

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