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| | ==PyrR of Mycobacterium Tuberculosis as a potential drug target== | | ==PyrR of Mycobacterium Tuberculosis as a potential drug target== |
| - | <StructureSection load='1w30' size='340' side='right' caption='[[1w30]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='1w30' size='340' side='right'caption='[[1w30]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1w30]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W30 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1w30]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W30 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uracil_phosphoribosyltransferase Uracil phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.9 2.4.2.9] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w30 OCA], [http://pdbe.org/1w30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w30 RCSB], [http://www.ebi.ac.uk/pdbsum/1w30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w30 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w30 OCA], [https://pdbe.org/1w30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w30 RCSB], [https://www.ebi.ac.uk/pdbsum/1w30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w30 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PYRR_MYCTU PYRR_MYCTU]] Regulates the transcription of the pyrimidine nucleotide (pyr) operon in response to exogenous pyrimidines (By similarity). Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant (By similarity). | + | [https://www.uniprot.org/uniprot/PYRR_MYCTU PYRR_MYCTU] Regulates the transcription of the pyrimidine nucleotide (pyr) operon in response to exogenous pyrimidines (By similarity). Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Phosphoribosyltransferase|Phosphoribosyltransferase]] | + | *[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Uracil phosphoribosyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Castro, P]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Kantardjieff, K A]] | + | [[Category: Castro P]] |
| - | [[Category: Kim, C Y]] | + | [[Category: Kantardjieff KA]] |
| - | [[Category: Lekin, T]] | + | [[Category: Kim C-Y]] |
| - | [[Category: Rho, B S]] | + | [[Category: Lekin T]] |
| - | [[Category: Rupp, B]] | + | [[Category: Rho B-S]] |
| - | [[Category: Segelke, B W]] | + | [[Category: Rupp B]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Segelke BW]] |
| - | [[Category: Terwilliger, T]] | + | [[Category: Terwilliger T]] |
| - | [[Category: Vasquez, C]] | + | [[Category: Vasquez C]] |
| - | [[Category: Warfel, N N]] | + | [[Category: Warfel NN]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Pyrr]]
| + | |
| - | [[Category: Tb]]
| + | |
| - | [[Category: Tbsgc]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
PYRR_MYCTU Regulates the transcription of the pyrimidine nucleotide (pyr) operon in response to exogenous pyrimidines (By similarity). Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Mycobacterium tuberculosis pyrR gene (Rv1379) encodes a protein that regulates the expression of pyrimidine-nucleotide biosynthesis (pyr) genes in a UMP-dependent manner. Because pyrimidine biosynthesis is an essential step in the progression of TB, the gene product pyrR is an attractive antitubercular drug target. The 1.9 A native structure of Mtb pyrR determined by the TB Structural Genomics Consortium facilities in trigonal space group P3(1)21 is reported, with unit-cell parameters a = 66.64, c = 154.72 A at 120 K and two molecules in the asymmetric unit. The three-dimensional structure and residual uracil phosphoribosyltransferase activity point to a common PRTase ancestor for pyrR. However, while PRPP- and UMP-binding sites have been retained in Mtb pyrR, a distinct dimer interaction among subunits creates a deep positively charged cleft capable of binding pyr mRNA. In silico screening of pyrimidine-nucleoside analogs has revealed a number of potential lead compounds that, if bound to Mtb pyrR, could facilitate transcriptional attenuation, particularly cyclopentenyl nucleosides.
Structure of pyrR (Rv1379) from Mycobacterium tuberculosis: a persistence gene and protein drug target.,Kantardjieff KA, Vasquez C, Castro P, Warfel NM, Rho BS, Lekin T, Kim CY, Segelke BW, Terwilliger TC, Rupp B Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):355-64. Epub 2005, Mar 24. PMID:15805589[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kantardjieff KA, Vasquez C, Castro P, Warfel NM, Rho BS, Lekin T, Kim CY, Segelke BW, Terwilliger TC, Rupp B. Structure of pyrR (Rv1379) from Mycobacterium tuberculosis: a persistence gene and protein drug target. Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):355-64. Epub 2005, Mar 24. PMID:15805589 doi:10.1107/S090744490403389X
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