2oi2: Difference between revisions

Revision as of 14:40, 29 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:2oi2.png

Template:STRUCTURE 2oi2

Streptococcus pneumoniae Mevalonate Kinase in Complex with DiphosphomevalonateStreptococcus pneumoniae Mevalonate Kinase in Complex with Diphosphomevalonate

Template:ABSTRACT PUBMED 17400916

About this StructureAbout this Structure

2OI2 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the Streptococcus pneumoniae mevalonate kinase in complex with diphosphomevalonate., Andreassi JL 2nd, Bilder PW, Vetting MW, Roderick SL, Leyh TS, Protein Sci. 2007 May;16(5):983-9. Epub 2007 Mar 30. PMID:17400916

Page seeded by OCA on Tue Jul 29 14:40:04 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2oi2.jpg|left|200px]]
+{{Seed}}
+[[Image:2oi2.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2oi2|  PDB=2oi2  |  SCENE=  }}
-'''Streptococcus pneumoniae Mevalonate Kinase in Complex with Diphosphomevalonate'''
+===Streptococcus pneumoniae Mevalonate Kinase in Complex with Diphosphomevalonate===
-==Overview==
+<!--
-Streptococcus pneumoniae, a ubiquitous gram-positive pathogen with an alarming, steadily evolving resistance to frontline antimicrobials, poses a severe global health threat both in the community and in the clinic. The recent discovery that diphosphomevalonate (DPM), an essential intermediate in the isoprenoid biosynthetic pathway, potently and allosterically inhibits S. pneumoniae mevalonate kinase (SpMK) without affecting the human isozyme established a new target and lead compound for antimicrobial design. Here we present the crystal structure of the first S. pneumoniae mevalonate kinase, at a resolution of 2.5 A and in complex with DPM.Mg(2+) in the active-site cleft. Structural comparison of SpMK with other members of the GHMP kinase family reveals that DPM functions as a partial bisubstrate analog (mevalonate linked to the pyrophosphoryl moiety of ATP) in that it elicits a ternary-complexlike form of the enzyme, except for localized disordering in a region that would otherwise interact with the missing portion of the nucleotide. Features of the SpMK-binding pockets are discussed in the context of established mechanistic findings and inherited human diseases linked to MK deficiency.
+The line below this paragraph, {{ABSTRACT_PUBMED_17400916}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17400916 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17400916}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Vetting, M W.]]
 [[Category: Enzyme-inhibitor complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 10:57:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:40:04 2008''