1rea
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.99.37 3.4.99.37] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.99.37 3.4.99.37] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rea OCA], [http://www.ebi.ac.uk/pdbsum/1rea PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rea RCSB]</span> | ||
}} | }} | ||
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[[Category: Steitz, T A.]] | [[Category: Steitz, T A.]] | ||
[[Category: Story, R M.]] | [[Category: Story, R M.]] | ||
| - | [[Category: ADP]] | ||
[[Category: homologous recombination]] | [[Category: homologous recombination]] | ||
[[Category: self-cleavage stimulation]] | [[Category: self-cleavage stimulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:27:01 2008'' |
Revision as of 20:27, 30 March 2008
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| , resolution 2.7Å | |||||||
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| Ligands: | |||||||
| Activity: | Deleted entry, with EC number 3.4.99.37 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE RECA PROTEIN-ADP COMPLEX
Overview
The recA protein catalyses the ATP-driven homologous pairing and strand exchange of DNA molecules. It is an allosteric enzyme: the ATPase activity is DNA-dependent, and ATP-bound recA protein has a high affinity for DNA, whereas the ADP-bound form has a low affinity. In the absence of ATP hydrolysis, recA protein can still promote homologous pairing, apparently through the formation of a triple-stranded intermediate. The exact role of ATP hydrolysis is not clear, but it presumably drives the triplex intermediate towards products. Here we determine the position of bound ADP diffused into the recA crystal. We show that only the phosphates are bound in the same way as in other NTPases containing the G/AXXXXGKT/S motif. We propose that recA protein may change its conformation upon ATP hydrolysis in a manner analogous to one such protein, the p21 protein from the ras oncogene. A model is presented to account for the allosteric stimulation of DNA binding by ATP. The mechanism by which nucleoside triphosphate hydrolysis is coupled to the binding of another ligand in recA protein and p21 may be typical of the large class of NTPases containing this conserved motif.
About this Structure
1REA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the recA protein-ADP complex., Story RM, Steitz TA, Nature. 1992 Jan 23;355(6358):374-6. PMID:1731253
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