2jc3

From Proteopedia

Revision as of 15:24, 30 October 2007

STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE B FROM SALMONELLA TYPHIMURIUM

Overview

O-Acetylserine sulfhydrylase is a pyridoxal 5'-phosphate-dependent enzyme, that catalyzes the final step in the cysteine biosynthetic pathway in, enteric bacteria and plants, the replacement of the beta-acetoxy group of, O-acetyl-l-serine by a thiol to give l-cysteine. Two isozymes are found in, Salmonella typhimurium, with the A-isozyme expressed under aerobic and the, B-isozyme expressed under anaerobic conditions. The structure of, O-acetylserine sulfhydrylase B has been solved to 2.3 A and exhibits, overall a fold very similar to that of the A-isozyme. The main difference, between the two isozymes is the more hydrophilic active site of the, B-isozyme with two ionizable residues, C280 and D281, replacing the, neutral residues S300 and P299, respectively, in the A-isozyme. D281 is, ... [(full description)]

About this Structure

2JC3 is a [Single protein] structure of sequence from [Salmonella typhimurium] with PLP as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structure, Mechanism, and Conformational Dynamics of O-Acetylserine Sulfhydrylase from Salmonella typhimurium: Comparison of A and B Isozymes., Chattopadhyay A, Meier M, Ivaninskii S, Burkhard P, Speroni F, Campanini B, Bettati S, Mozzarelli A, Rabeh WM, Li L, Cook PF, Biochemistry. 2007 Jul 17;46(28):8315-30. Epub 2007 Jun 21. PMID:17583914

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