1usy

From Proteopedia

Revision as of 14:05, 30 October 2007

ATP PHOSPHORIBOSYL TRANSFERASE (HISG:HISZ) COMPLEX FROM THERMOTOGA MARITIMA

Overview

The molecular structure of the ATP phosphoribosyl transferase from the, hyperthermophile Thermotoga maritima is composed of a 220 kDa, hetero-octameric complex comprising four catalytic subunits (HisGS) and, four regulatory subunits (HisZ). Steady-state kinetics indicate that only, the complete octameric complex is active and non-competitively inhibited, by the pathway product histidine. The rationale for these findings is, provided by the crystal structure revealing a total of eight histidine, binding sites that are located within each of the four HisGS-HisZ subunit, interfaces formed by the ATP phosphoribosyl transferase complex. While the, structure of the catalytic HisGS subunit is related to the catalytic, domain of another family of (HisGL)2 ATP phosphoribosyl transferases that, is ... [(full description)]

About this Structure

1USY is a [Protein complex] structure of sequences from [Thermotoga maritima] with PO4, HIS and HIS as [ligands]. Active as [ATP phosphoribosyltransferase], with EC number [2.4.2.17]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like subunit., Vega MC, Zou P, Fernandez FJ, Murphy GE, Sterner R, Popov A, Wilmanns M, Mol Microbiol. 2005 Feb;55(3):675-86. PMID:15660995

Page seeded by OCA on Tue Oct 30 16:10:25 2007