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1rea

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Revision as of 08:05, 28 February 2018

STRUCTURE OF THE RECA PROTEIN-ADP COMPLEX

Structural highlights

1rea is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. The April 2014 RCSB PDB Molecule of the Month feature on RecA and Rad51 by David Goodsell is 10.2210/rcsb_pdb/mom_2014_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RECA_ECOLI] Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.[HAMAP-Rule:MF_00268]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structure of the recA protein-ADP complex.,Story RM, Steitz TA Nature. 1992 Jan 23;355(6358):374-6. PMID:1731253^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Story RM, Steitz TA. Structure of the recA protein-ADP complex. Nature. 1992 Jan 23;355(6358):374-6. PMID:1731253 doi:http://dx.doi.org/10.1038/355374a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rea"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF THE RECA PROTEIN-ADP COMPLEX==
 <StructureSection load='1rea' size='340' side='right' caption='[[1rea]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1rea]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The April 2014 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''RecA and Rad51''  by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2014_4 10.2210/rcsb_pdb/mom_2014_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1REA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1REA FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1rea PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rea RCSB], [http://www.ebi.ac.uk/pdbsum/1rea PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1rea PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rea RCSB], [http://www.ebi.ac.uk/pdbsum/1rea PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rea ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/1rea_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/1rea_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1rea

From Proteopedia

Revision as of 08:05, 28 February 2018

STRUCTURE OF THE RECA PROTEIN-ADP COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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