1p4a

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{{STRUCTURE_1p4a| PDB=1p4a | SCENE= }}
{{STRUCTURE_1p4a| PDB=1p4a | SCENE= }}
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'''Crystal Structure of the PurR complexed with cPRPP'''
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===Crystal Structure of the PurR complexed with cPRPP===
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==Overview==
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Bacillus subtilis PurR represses transcription of several genes involved in purine synthesis, metabolism, and transport and cofactor synthesis. PurR binds specifically to DNAs containing an inverted repeat of a 14-nucleotide "PurBox" located in the upstream control regions of genes in the PurR regulon. Further biochemical investigation of the interaction of PurR with a series of shortened upstream DNA fragments of the pur operon determined the minimum length and specificity elements of the operator. The relative affinities of the two PurBoxes differ significantly, such that upstream PurBox1 (-81 to -68 relative to the transcription start site) is designated "strong" and downstream PurBox2 (-49 to -36) is designated "weak." Two PurBoxes are required for high-affinity PurR binding, and one of these must be strong. The shortest DNA construct with high affinity for PurR is a 74-bp perfect palindrome in which weak PurBox2 and its flanking sequences are replaced by strong PurBox1 and flanking sequences. Two PurR dimers bind to this symmetric construct. Phosphoribosylpyrophosphate (PRPP), the effector molecule that reduces affinity of PurR for DNA, requires one weak PurBox in the DNA construct to inhibit PurR binding. PRPP binds, as expected, to a PRPP-motif in PurR. A tracks outside the central conserved CGAA sequence of the PurBox may facilitate DNA bending, leading to a proposal for strong and weak designations of PurBoxes in the control regions of other genes regulated by PurR.
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==About this Structure==
==About this Structure==
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[[Category: Zhu, J.]]
[[Category: Zhu, J.]]
[[Category: Transcription]]
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Revision as of 10:28, 28 July 2008

Template:STRUCTURE 1p4a

Crystal Structure of the PurR complexed with cPRPP

Template:ABSTRACT PUBMED 12837784

About this Structure

1P4A is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Functional dissection of the Bacillus subtilis pur operator site., Bera AK, Zhu J, Zalkin H, Smith JL, J Bacteriol. 2003 Jul;185(14):4099-109. PMID:12837784

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