2nsf
From Proteopedia
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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 2.05A, 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 His(52), Glu(144), and, His(148) 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.
About this Structure
2NSF is a Single protein structure of sequence from Corynebacterium glutamicum with , and as ligands. Active as Maleylpyruvate isomerase, with EC number 5.2.1.4 Full crystallographic information is available from OCA.
Reference
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):16288-5294. Epub 2007 Apr 11. PMID:17428791
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