2ovg: Difference between revisions

Revision as of 19:50, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ovg.png

Template:STRUCTURE 2ovg

Lambda Cro Q27P/A29S/K32Q triple mutant at 1.35 A in space group P3221Lambda Cro Q27P/A29S/K32Q triple mutant at 1.35 A in space group P3221

Template:ABSTRACT PUBMED 18054042

About this StructureAbout this Structure

2OVG is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

ReferenceReference

Two structures of a lambda Cro variant highlight dimer flexibility but disfavor major dimer distortions upon specific binding of cognate DNA., Hall BM, Roberts SA, Heroux A, Cordes MH, J Mol Biol. 2008 Jan 18;375(3):802-11. Epub 2007 Nov 6. PMID:18054042

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-'''Lambda Cro Q27P/A29S/K32Q triple mutant at 1.35 A in space group P3221'''
+===Lambda Cro Q27P/A29S/K32Q triple mutant at 1.35 A in space group P3221===
-==Overview==
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-Previously reported crystal structures of free and DNA-bound dimers of lambda Cro differ strongly (about 4 A backbone rmsd), suggesting both flexibility of the dimer interface and induced-fit protein structure changes caused by sequence-specific DNA binding. Here, we present two crystal structures, in space groups P3(2)21 and C2 at 1.35 and 1.40 A resolution, respectively, of a variant of lambda Cro with three mutations in its recognition helix (Q27P/A29S/K32Q, or PSQ for short). One dimer structure (P3(2)21; PSQ form 1) resembles the DNA-bound wild-type Cro dimer (1.0 A backbone rmsd), while the other (C2; PSQ form 2) resembles neither unbound (3.6 A) nor bound (2.4 A) wild-type Cro. Both PSQ form 2 and unbound wild-type dimer crystals have a similar interdimer beta-sheet interaction between the beta1 strands at the edges of the dimer. In the former, an infinite, open beta-structure along one crystal axis results, while in the latter, a closed tetrameric barrel is formed. Neither the DNA-bound wild-type structure nor PSQ form 1 contains these interdimer interactions. We propose that beta-sheet superstructures resulting from crystal contact interactions distort Cro dimers from their preferred solution conformation, which actually resembles the DNA-bound structure. These results highlight the remarkable flexibility of lambda Cro but also suggest that sequence-specific DNA binding may not induce large changes in the protein structure.
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 ==About this Structure==
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 [[Category: Helix-turn-helix]]
 [[Category: Transcription factor]]
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