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1O57

CRYSTAL STRUCTURE OF THE PURINE OPERON REPRESSOR OF BACILLUS SUBTILIS

Replaces:  1P41
Summary for 1O57
Entry DOI10.2210/pdb1o57/pdb
DescriptorPUR OPERON REPRESSOR, SULFATE ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (8 entities in total)
Functional Keywordspurine operon repressor, helix-turn-helix domain, phosphoribosyltranseferases, domain recombination, dna binding, transcription regulation, dna binding protein
Biological sourceBacillus subtilis
Total number of polymer chains4
Total formula weight131254.13
Authors
Sinha, S.C.,Krahn, J.,Shin, B.S.,Tomchick, D.R.,Zalkin, H.,Smith, J.L. (deposition date: 2003-04-20, release date: 2003-08-26, Last modification date: 2023-12-27)
Primary citationSinha, S.C.,Krahn, J.,Shin, B.S.,Tomchick, D.R.,Zalkin, H.,Smith, J.L.
The Purine Repressor of Bacillus Subtilis: A Novel Combination of Domains Adapted for Transcription Regulation
J.Bacteriol., 185:4087-4098, 2003
Cited by
PubMed Abstract: The purine repressor from Bacillus subtilis, PurR, represses transcription from a number of genes with functions in the synthesis, transport, and metabolism of purines. The 2.2-A crystal structure of PurR reveals a two-domain protein organized as a dimer. The larger C-terminal domain belongs to the PRT structural family, in accord with a sequence motif for binding the inducer phosphoribosylpyrophosphate (PRPP). The PRT domain is fused to a smaller N-terminal domain that belongs to the winged-helix family of DNA binding proteins. A positively charged surface on the winged-helix domain likely binds specific DNA sequences in the recognition site. A second positively charged surface surrounds the PRPP site at the opposite end of the PurR dimer. Conserved amino acids in the sequences of PurR homologs in 21 gram-positive bacteria cluster on the proposed recognition surface of the winged-helix domain and around the PRPP binding site at the opposite end of the molecule, supporting a common function of DNA and PRPP binding for all of the proteins. The structure supports a binding mechanism in which extended regions of DNA interact with extensive protein surface. Unlike most PRT proteins, which are phosphoribosyltransferases (PRTases), PurR lacks catalytic activity. This is explained by a tyrosine side chain that blocks the site for a nucleophile cosubstrate in PRTases. Thus, B. subtilis has adapted an enzyme fold to serve as an effector-binding domain and has used it in a novel combination with the DNA-binding winged-helix domain as a repressor of purine genes.
PubMed: 12837783
DOI: 10.1128/JB.185.14.4087-4098.2003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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