Purine repressor: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
The PurP guanine co-repressor binding site includes stacking interactions as well as hydrogen bonded ones. The DNA binding domain contains a helix-turn-helix-loop-helix motif which interacts with the DNA major groove and a hinge helix binding to to the DNA minor groove.  Residue L53 interdigitates with the DNA central base pair<ref>PMID:9278422</ref>.
The <scene name='55/554904/Cv/2'>PurP guanine co-repressor binding site includes stacking interactions as well as hydrogen bonded ones</scene>. Water molecules shown as red spheres. The DNA binding domain contains a helix-turn-helix-loop-helix motif which interacts with the DNA major groove and a hinge helix binding to to the DNA minor groove.  Residue L53 interdigitates with the DNA central base pair<ref>PMID:9278422</ref>.
</StructureSection>
</StructureSection>



Revision as of 14:34, 31 July 2016

Function

Purine repressor (PurR) is a member of the lac repressor family. PurP binds DNA via a highly conserved helix-turn-helix at the N terminal (DBD). PurP contains a nucleotide co-repressor binding domain as well (CBD). PurP binds to a 16-bp operator sequence and co-regulates genes which are involved in the biosynthesis of purine and pyrimidine nucleotides[1].

Structural highlights

The . Water molecules shown as red spheres. The DNA binding domain contains a helix-turn-helix-loop-helix motif which interacts with the DNA major groove and a hinge helix binding to to the DNA minor groove. Residue L53 interdigitates with the DNA central base pair[2].

Structure of

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3D structures of purine repressor3D structures of purine repressor

Updated on 31-July-2016

ReferencesReferences

  1. Wilson HR, Turnbough CL Jr. Role of the purine repressor in the regulation of pyrimidine gene expression in Escherichia coli K-12. J Bacteriol. 1990 Jun;172(6):3208-13. PMID:1971621
  2. Schumacher MA, Glasfeld A, Zalkin H, Brennan RG. The X-ray structure of the PurR-guanine-purF operator complex reveals the contributions of complementary electrostatic surfaces and a water-mediated hydrogen bond to corepressor specificity and binding affinity. J Biol Chem. 1997 Sep 5;272(36):22648-53. PMID:9278422

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