2nsf: Difference between revisions

Revision as of 13:53, 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:2nsf.png

Template:STRUCTURE 2nsf

Crystal structure of the mycothiol-dependent maleylpyruvate isomeraseCrystal structure of the mycothiol-dependent maleylpyruvate isomerase

Template:ABSTRACT PUBMED 17428791

About this StructureAbout this Structure

2NSF is a Single protein structure of sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures and site-directed mutagenesis of a mycothiol-dependent enzyme reveal a novel folding and molecular basis for mycothiol-mediated maleylpyruvate isomerization., Wang R, Yin YJ, Wang F, Li M, Feng J, Zhang HM, Zhang JP, Liu SJ, Chang WR, J Biol Chem. 2007 Jun 1;282(22):16288-294. Epub 2007 Apr 11. PMID:17428791

Page seeded by OCA on Tue Jul 29 13:53:40 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2nsf.gif|left|200px]]
+{{Seed}}
+[[Image:2nsf.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2nsf|  PDB=2nsf  |  SCENE=  }}
-'''Crystal structure of the mycothiol-dependent maleylpyruvate isomerase'''
+===Crystal structure of the mycothiol-dependent maleylpyruvate isomerase===
-==Overview==
+<!--
-Mycothiol (MSH) is the major low molecular mass thiols in many Gram-positive bacteria such as Mycobacterium tuberculosis and Corynebacterium glutamicum. The physiological roles of MSH are believed to be equivalent to those of GSH in Gram-negative bacteria, but current knowledge of MSH is limited to detoxification of alkalating chemicals and protection from host cell defense/killing systems. Recently, an MSH-dependent maleylpyruvate isomerase (MDMPI) was discovered from C. glutamicum, and this isomerase represents one example of many putative MSH-dependent enzymes that take MSH as cofactor. In this report, fourteen mutants of MDMPI were generated. The wild type and mutant (H52A) MDMPIs were crystallized and their structures were solved at 1.75 and 2.05 A resolution, respectively. The crystal structures reveal that this enzyme contains a divalent metal-binding domain and a C-terminal domain possessing a novel folding pattern (alphabetaalphabetabetaalpha fold). The divalent metal-binding site is composed of residues His52, Glu144, and His148 and is located at the bottom of a surface pocket. Combining the structural and site-directed mutagenesis studies, it is proposed that this surface pocket including the metal ion and MSH moiety formed the putative catalytic center.
+The line below this paragraph, {{ABSTRACT_PUBMED_17428791}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17428791 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17428791}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Wang, R.]]
 [[Category: Metal binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:51:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:53:40 2008''