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1NON

PyrR, the regulator of the pyrimidine biosynthetic operon in Bacillus caldolyticus

Summary for 1NON
Entry DOI10.2210/pdb1non/pdb
Related1A3C
DescriptorPyrR bifunctional protein (2 entities in total)
Functional Keywordstranscription regulation; attenuation protein; rna-binding protein; pyrimidine biosynthesis; transferase; prtase; uracil phosphoribosyltransferase; bifunctional enzyme, transcription, transferase
Biological sourceBacillus caldolyticus
Total number of polymer chains4
Total formula weight79868.20
Authors
Switzer, R.L.,Chander, P.,Smith, J.L.,Halbig, K.M.,Miller, J.K.,Bonner, H.K.,Grabner, G.K. (deposition date: 2003-01-16, release date: 2004-05-25, Last modification date: 2023-08-16)
Primary citationChander, P.,Halbig, K.M.,Miller, J.K.,Fields, C.J.,Bonner, H.K.,Grabner, G.K.,Switzer, R.L.,Smith, J.L.
Structure of the Nucleotide Complex of PyrR, the pyr Attenuation Protein from Bacillus caldolyticus, Suggests Dual Regulation by Pyrimidine and Purine Nucleotides
J.Bacteriol., 187:1773-1782, 2005
Cited by
PubMed: 15716449
DOI: 10.1128/JB.187.5.1773-1782.2005
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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