1rea
From Proteopedia
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| - | [[Image:1rea.jpg|left|200px]] | + | [[Image:1rea.jpg|left|200px]] |
| - | + | ||
| - | '''STRUCTURE OF THE RECA PROTEIN-ADP COMPLEX''' | + | {{Structure |
| + | |PDB= 1rea |SIZE=350|CAPTION= <scene name='initialview01'>1rea</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE RECA PROTEIN-ADP COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1REA is a [ | + | 1REA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1REA OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the recA protein-ADP complex., Story RM, Steitz TA, Nature. 1992 Jan 23;355(6358):374-6. PMID:[http:// | + | Structure of the recA protein-ADP complex., Story RM, Steitz TA, Nature. 1992 Jan 23;355(6358):374-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1731253 1731253] |
[[Category: Deleted entry]] | [[Category: Deleted entry]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: self-cleavage stimulation]] | [[Category: self-cleavage stimulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:50:26 2008'' |
Revision as of 11:50, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Ligands: | |||||||
| Activity: | Deleted entry, with EC number 3.4.99.37 | ||||||
| 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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