2bke
From Proteopedia
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|PDB= 2bke |SIZE=350|CAPTION= <scene name='initialview01'>2bke</scene>, resolution 3.200Å | |PDB= 2bke |SIZE=350|CAPTION= <scene name='initialview01'>2bke</scene>, resolution 3.200Å | ||
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bke OCA], [http://www.ebi.ac.uk/pdbsum/2bke PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bke RCSB]</span> | ||
}} | }} | ||
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[[Category: Richard, D L.]] | [[Category: Richard, D L.]] | ||
[[Category: White, M F.]] | [[Category: White, M F.]] | ||
| - | [[Category: CL]] | ||
[[Category: archaea]] | [[Category: archaea]] | ||
[[Category: dna repair]] | [[Category: dna repair]] | ||
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[[Category: sulfolobus solfataricus]] | [[Category: sulfolobus solfataricus]] | ||
| - | ''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 02:07:44 2008'' |
Revision as of 23:07, 30 March 2008
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| , resolution 3.200Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CONFORMATIONAL FLEXIBILITY REVEALED BY THE CRYSTAL STRUCTURE OF A CRENARCHAEAL RADA
Overview
Homologous recombinational repair is an essential mechanism for repair of double-strand breaks in DNA. Recombinases of the RecA-fold family play a crucial role in this process, forming filaments that utilize ATP to mediate their interactions with single- and double-stranded DNA. The recombinase molecules present in the archaea (RadA) and eukaryota (Rad51) are more closely related to each other than to their bacterial counterpart (RecA) and, as a result, RadA makes a suitable model for the eukaryotic system. The crystal structure of Sulfolobus solfataricus RadA has been solved to a resolution of 3.2 A in the absence of nucleotide analogues or DNA, revealing a narrow filamentous assembly with three molecules per helical turn. As observed in other RecA-family recombinases, each RadA molecule in the filament is linked to its neighbour via interactions of a short beta-strand with the neighbouring ATPase domain. However, despite apparent flexibility between domains, comparison with other structures indicates conservation of a number of key interactions that introduce rigidity to the system, allowing allosteric control of the filament by interaction with ATP. Additional analysis reveals that the interaction specificity of the five human Rad51 paralogues can be predicted using a simple model based on the RadA structure.
About this Structure
2BKE is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA., Ariza A, Richard DJ, White MF, Bond CS, Nucleic Acids Res. 2005 Mar 8;33(5):1465-73. Print 2005. PMID:15755748
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