1nh8
|
ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH AMP AND HISTIDINE
OverviewOverview
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 StructureAbout this Structure
1NH8 is a Single protein structure of sequence from Mycobacterium tuberculosis with , and as ligands. Active as ATP phosphoribosyltransferase, with EC number 2.4.2.17 Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Thu Feb 21 14:06:05 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- ATP phosphoribosyltransferase
- Mycobacterium tuberculosis
- Single protein
- Cho, Y.
- Sacchettini, J C.
- Sharma, V.
- TBSGC, TB Structural Genomics Consortium.
- AMP
- HIS
- SO4
- Atp
- De novo his biosynthesis
- Phosphoribosyltransferase
- Protein structure initiative
- Prpp
- Prtase
- Psi
- Structural genomics
- Tb structural genomics consortium
- Tbsgc
- Transferase