1nh7: Difference between revisions
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam08029 HisG_C], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK00489 hisG], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01634 HisG]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam08029 HisG_C], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK00489 hisG], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01634 HisG]</span> | ||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nh7 OCA], [http://www.ebi.ac.uk/pdbsum/1nh7 PDBsum | |RELATEDENTRY=[[1nh8|1NH8]] | ||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nh7 OCA], [http://www.ebi.ac.uk/pdbsum/1nh7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nh7 RCSB]</span> | |||
}} | }} | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:30:19 2008'' | ||
Revision as of 22:30, 30 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | ATP phosphoribosyltransferase, with EC number 2.4.2.17 | ||||||
| Domains: | HisG_C, hisG, HisG | ||||||
| Related: | 1NH8
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS
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
1NH7 is a Single protein structure of sequence from Mycobacterium tuberculosis. 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
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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.
- Atp
- De novo his biosynthesis
- Phosphoribosyltransferase
- Protein structure initiative
- Prpp
- Prtase
- Psi
- Structural genomic
- Tb structural genomics consortium
- Tbsgc
- Transferase