1NON
PyrR, the regulator of the pyrimidine biosynthetic operon in Bacillus caldolyticus
Summary for 1NON
Entry DOI | 10.2210/pdb1non/pdb |
Related | 1A3C |
Descriptor | PyrR bifunctional protein (2 entities in total) |
Functional Keywords | transcription regulation; attenuation protein; rna-binding protein; pyrimidine biosynthesis; transferase; prtase; uracil phosphoribosyltransferase; bifunctional enzyme, transcription, transferase |
Biological source | Bacillus caldolyticus |
Total number of polymer chains | 4 |
Total formula weight | 79868.20 |
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 citation | Chander, 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: 15716449DOI: 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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