1NH8

ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH AMP AND HISTIDINE

Summary for 1NH8

• Entry DOI: 10.2210/pdb1nh8/pdb
• Related: 1NH7
• Descriptor: ATP Phosphoribosyltransferase, SULFATE ION, ADENOSINE MONOPHOSPHATE, ... (5 entities in total)
• Functional Keywords: prtase, de novo his biosynthesis, prpp, transferase, phosphoribosyltransferase, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc
• Biological source: Mycobacterium tuberculosis H37Rv
• Cellular location: Cytoplasm (By similarity): P60759
• Total number of polymer chains: 1
• Total formula weight: 33475.65

Authors

Cho, Y.,Sharma, V.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2002-12-18, release date: 2003-02-11, Last modification date: 2024-12-25)

Primary citation

Cho, Y.,Sharma, V.,Sacchettini, J.C.
Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis
J.Biol.Chem., 278:8333-, 2003

PubMed Abstract: 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.

PubMed: 12511575
DOI: 10.1074/jbc.M212124200

Experimental method

X-RAY DIFFRACTION (1.8 Å)