2z2p: Difference between revisions

Revision as of 19:26, 28 July 2008

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File:2z2p.png

Template:STRUCTURE 2z2p

Crystal Structure of catalytically inactive H270A virginiamycin B lyase from Staphylococcus aureus with QuinupristinCrystal Structure of catalytically inactive H270A virginiamycin B lyase from Staphylococcus aureus with Quinupristin

Template:ABSTRACT PUBMED 17563376

About this StructureAbout this Structure

2Z2P is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for streptogramin B resistance in Staphylococcus aureus by virginiamycin B lyase., Korczynska M, Mukhtar TA, Wright GD, Berghuis AM, Proc Natl Acad Sci U S A. 2007 Jun 19;104(25):10388-93. Epub 2007 Jun 11. PMID:17563376

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OCA

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-'''Crystal Structure of catalytically inactive H270A virginiamycin B lyase from Staphylococcus aureus with Quinupristin'''
+===Crystal Structure of catalytically inactive H270A virginiamycin B lyase from Staphylococcus aureus with Quinupristin===
-==Overview==
+<!--
-The streptogramin combination therapy of quinupristin-dalfopristin (Synercid) is used to treat infections caused by bacterial pathogens, such as methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus faecium. However, the effectiveness of this therapy is being compromised because of an increased incidence of streptogramin resistance. One of the clinically observed mechanisms of resistance is enzymatic inactivation of the type B streptogramins, such as quinupristin, by a streptogramin B lyase, i.e., virginiamycin B lyase (Vgb). The enzyme catalyzes the linearization of the cyclic antibiotic via a cleavage that requires a divalent metal ion. Here, we present crystal structures of Vgb from S. aureus in its apoenzyme form and in complex with quinupristin and Mg2+ at 1.65- and 2.8-A resolution, respectively. The fold of the enzyme is that of a seven-bladed beta-propeller, although the sequence reveals no similarity to other known members of this structural family. Quinupristin binds to a large depression on the surface of the enzyme, where it predominantly forms van der Waals interactions. Validated by site-directed mutagenesis studies, a reaction mechanism is proposed in which the initial abstraction of a proton is facilitated by a Mg2+ -linked conjugated system. Analysis of the Vgb-quinupristin structure and comparison with the complex between quinupristin and its natural target, the 50S ribosomal subunit, reveals features that can be exploited for developing streptogramins that are impervious to Vgb-mediated resistance.
+The line below this paragraph, {{ABSTRACT_PUBMED_17563376}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17563376 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17563376}}
 ==About this Structure==
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 [[Category: Virginiamycin b hydrolase]]
 [[Category: Virginiamycin b lyase]]
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