1non
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1non.gif|left|200px]] | + | [[Image:1non.gif|left|200px]] |
| - | + | ||
| - | '''PyrR, the regulator of the pyrimidine biosynthetic operon in Bacillus caldolyticus''' | + | {{Structure |
| + | |PDB= 1non |SIZE=350|CAPTION= <scene name='initialview01'>1non</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= pyrr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1394 Bacillus caldolyticus]) | ||
| + | }} | ||
| + | |||
| + | '''PyrR, the regulator of the pyrimidine biosynthetic operon in Bacillus caldolyticus''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1NON is a [ | + | 1NON is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_caldolyticus Bacillus caldolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NON OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the nucleotide complex of PyrR, the pyr attenuation protein from Bacillus caldolyticus, suggests dual regulation by pyrimidine and purine nucleotides., Chander P, Halbig KM, Miller JK, Fields CJ, Bonner HK, Grabner GK, Switzer RL, Smith JL, J Bacteriol. 2005 Mar;187(5):1773-82. PMID:[http:// | + | Structure of the nucleotide complex of PyrR, the pyr attenuation protein from Bacillus caldolyticus, suggests dual regulation by pyrimidine and purine nucleotides., Chander P, Halbig KM, Miller JK, Fields CJ, Bonner HK, Grabner GK, Switzer RL, Smith JL, J Bacteriol. 2005 Mar;187(5):1773-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15716449 15716449] |
[[Category: Bacillus caldolyticus]] | [[Category: Bacillus caldolyticus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 23: | Line 32: | ||
[[Category: transcription regulation; attenuation protein; rna-binding protein; pyrimidine biosynthesis; transferase; prtase; uracil phosphoribosyltransferase; bifunctional enzyme]] | [[Category: transcription regulation; attenuation protein; rna-binding protein; pyrimidine biosynthesis; transferase; prtase; uracil phosphoribosyltransferase; bifunctional enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:59:35 2008'' |
Revision as of 10:59, 20 March 2008
| |||||||
| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | pyrr (Bacillus caldolyticus) | ||||||
| Activity: | Uracil phosphoribosyltransferase, with EC number 2.4.2.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PyrR, the regulator of the pyrimidine biosynthetic operon in Bacillus caldolyticus
Overview
PyrR is a protein that regulates the expression of genes and operons of pyrimidine nucleotide biosynthesis (pyr genes) in many bacteria. PyrR acts by binding to specific sequences on pyr mRNA and causing transcriptional attenuation when intracellular levels of uridine nucleotides are elevated. PyrR from Bacillus subtilis has been purified and extensively studied. In this work, we describe the purification to homogeneity and characterization of recombinant PyrR from the thermophile Bacillus caldolyticus and the crystal structures of unliganded PyrR and a PyrR-nucleotide complex. The B. caldolyticus pyrR gene was previously shown to restore normal regulation of the B. subtilis pyr operon in a pyrR deletion mutant. Like B. subtilis PyrR, B. caldolyticus PyrR catalyzes the uracil phosphoribosyltransferase reaction but with maximal activity at 60 degrees C. Crystal structures of B. caldolyticus PyrR reveal a dimer similar to the B. subtilis PyrR dimer and, for the first time, binding sites for nucleotides. UMP and GMP, accompanied by Mg2+, bind specifically to PyrR active sites. Nucleotide binding to PyrR is similar to other phosphoribosyltransferases, but Mg2+ binding differs. GMP binding was unexpected. The protein bound specific sequences of pyr RNA 100 to 1,000 times more tightly than B. subtilis PyrR, depending on the RNA tested and the assay method; uridine nucleotides enhanced RNA binding, but guanosine nucleotides antagonized it. The new findings of specific GMP binding and its antagonism of RNA binding suggest cross-regulation of the pyr operon by purines.
About this Structure
1NON is a Single protein structure of sequence from Bacillus caldolyticus. Full crystallographic information is available from OCA.
Reference
Structure of the nucleotide complex of PyrR, the pyr attenuation protein from Bacillus caldolyticus, suggests dual regulation by pyrimidine and purine nucleotides., Chander P, Halbig KM, Miller JK, Fields CJ, Bonner HK, Grabner GK, Switzer RL, Smith JL, J Bacteriol. 2005 Mar;187(5):1773-82. PMID:15716449
Page seeded by OCA on Thu Mar 20 12:59:35 2008
Categories: Bacillus caldolyticus | Single protein | Uracil phosphoribosyltransferase | Bonner, H K. | Chander, P. | Grabner, G K. | Halbig, K M. | Miller, J K. | Smith, J L. | Switzer, R L. | Transcription regulation; attenuation protein; rna-binding protein; pyrimidine biosynthesis; transferase; prtase; uracil phosphoribosyltransferase; bifunctional enzyme
