1nh7

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Image:1nh7.gif


PDB ID 1nh7

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, resolution 2.70Å
Ligands: ,
Activity: ATP phosphoribosyltransferase, with EC number 2.4.2.17
Domains: HisG_C, hisG, HisG
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS


Overview

The N-1-(5'-phosphoribosyl)-ATP transferase catalyzes the first step of the histidine biosynthetic pathway and is regulated by a feedback mechanism by the product histidine. The crystal structures of the N-1-(5'-phosphoribosyl)-ATP transferase from Mycobacterium tuberculosis in complex with inhibitor histidine and AMP has been determined to 1.8 A resolution and without ligands to 2.7 A resolution. The active enzyme exists primarily as a dimer, and the histidine-inhibited form is a hexamer. The structure represents a new fold for a phosphoribosyltransferase, consisting of three continuous domains. The inhibitor AMP binds in the active site cavity formed between the two catalytic domains. A model for the mechanism of allosteric inhibition has been derived from conformational differences between the AMP:His-bound and apo structures.

About this Structure

1NH7 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis., Cho Y, Sharma V, Sacchettini JC, J Biol Chem. 2003 Mar 7;278(10):8333-9. Epub 2003 Jan 2. PMID:12511575

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