2ovg: Difference between revisions
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|PDB= 2ovg |SIZE=350|CAPTION= <scene name='initialview01'>2ovg</scene>, resolution 1.350Å | |PDB= 2ovg |SIZE=350|CAPTION= <scene name='initialview01'>2ovg</scene>, resolution 1.350Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+111'>AC1</scene> and <scene name='pdbsite=AC2:Epe+Binding+Site+For+Residue+A+110'>AC2</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+111'>AC1</scene> and <scene name='pdbsite=AC2:Epe+Binding+Site+For+Residue+A+110'>AC2</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= cro ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Enterobacteria phage lambda]) | |GENE= cro ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Enterobacteria phage lambda]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2ecs|2ECS]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ovg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovg OCA], [http://www.ebi.ac.uk/pdbsum/2ovg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ovg RCSB]</span> | |||
}} | }} | ||
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[[Category: Heroux, A.]] | [[Category: Heroux, A.]] | ||
[[Category: Roberts, S A.]] | [[Category: Roberts, S A.]] | ||
[[Category: bacteriophage]] | [[Category: bacteriophage]] | ||
[[Category: flexibility]] | [[Category: flexibility]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:23:46 2008'' | ||
Revision as of 04:23, 31 March 2008
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| , resolution 1.350Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , | ||||||
| Gene: | cro (Enterobacteria phage lambda) | ||||||
| Related: | 2ECS
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Lambda Cro Q27P/A29S/K32Q triple mutant at 1.35 A in space group P3221
OverviewOverview
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.
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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