1non

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[[Image:1non.gif|left|200px]]
[[Image:1non.gif|left|200px]]
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{{Structure
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|PDB= 1non |SIZE=350|CAPTION= <scene name='initialview01'>1non</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_1non", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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or leave the SCENE parameter empty for the default display.
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|GENE= pyrr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1394 Bacillus caldolyticus])
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{{STRUCTURE_1non| PDB=1non | SCENE= }}
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|RELATEDENTRY=[[1a3c|1A3C]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1non FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1non OCA], [http://www.ebi.ac.uk/pdbsum/1non PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1non RCSB]</span>
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'''PyrR, the regulator of the pyrimidine biosynthetic operon in Bacillus caldolyticus'''
'''PyrR, the regulator of the pyrimidine biosynthetic operon in Bacillus caldolyticus'''
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[[Category: Smith, J L.]]
[[Category: Smith, J L.]]
[[Category: Switzer, R L.]]
[[Category: Switzer, R L.]]
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[[Category: attenuation protein]]
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[[Category: Attenuation protein]]
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[[Category: bifunctional enzyme]]
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[[Category: Bifunctional enzyme]]
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[[Category: prtase]]
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[[Category: Prtase]]
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[[Category: pyrimidine biosynthesis]]
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[[Category: Pyrimidine biosynthesis]]
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[[Category: rna-binding protein]]
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[[Category: Rna-binding protein]]
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[[Category: transcription regulation]]
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[[Category: Transcription regulation]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: uracil phosphoribosyltransferase]]
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[[Category: Uracil phosphoribosyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:47:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:33:15 2008''
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Revision as of 23:47, 2 May 2008

Image:1non.gif

Template:STRUCTURE 1non

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 Sat May 3 02:47:20 2008

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