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1w36

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Revision as of 07:50, 4 April 2018

RecBCD:DNA complex

Structural highlights

1w36 is a 8 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:
Activity:	Exodeoxyribonuclease V, with EC number 3.1.11.5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[EX5B_ECOLI] Required for efficient DNA repair; it catalyzes the unwinding of double-stranded DNA and the cleavage of single-stranded DNA and it stimulates local genetic recombination. All of these activities require concomitant hydrolysis of ATP. [EX5A_ECOLI] Exhibits several catalytic activities, including ATP-dependent exonuclease, ATP-stimulated endonuclease, ATP-dependent unwinding and DNA-dependent ATPase activities. Strand cleavage occurs 5' to 3' during the unwinding of duplex DNA at CHI sequences, which locally stimulate recombination. [EX5C_ECOLI] Exhibits a wide variety of catalytic activities including ATP-dependent exonuclease, ATP-stimulated endonuclease, ATP-dependent helicase and DNA-dependent ATPase activities.

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

RecBCD is a multi-functional enzyme complex that processes DNA ends resulting from a double-strand break. RecBCD is a bipolar helicase that splits the duplex into its component strands and digests them until encountering a recombinational hotspot (Chi site). The nuclease activity is then attenuated and RecBCD loads RecA onto the 3' tail of the DNA. Here we present the crystal structure of RecBCD bound to a DNA substrate. In this initiation complex, the DNA duplex has been split across the RecC subunit to create a fork with the separated strands each heading towards different helicase motor subunits. The strands pass along tunnels within the complex, both emerging adjacent to the nuclease domain of RecB. Passage of the 3' tail through one of these tunnels provides a mechanism for the recognition of a Chi sequence by RecC within the context of double-stranded DNA. Gating of this tunnel suggests how nuclease activity might be regulated.

Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks.,Singleton MR, Dillingham MS, Gaudier M, Kowalczykowski SC, Wigley DB Nature. 2004 Nov 11;432(7014):187-93. PMID:15538360^[1]

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

References

↑ Singleton MR, Dillingham MS, Gaudier M, Kowalczykowski SC, Wigley DB. Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks. Nature. 2004 Nov 11;432(7014):187-93. PMID:15538360 doi:10.1038/nature02988

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/1w36"

@@ Line 1: / Line 1: @@
-==RECBCD:DNA COMPLEX==
+==RecBCD:DNA complex==
 <StructureSection load='1w36' size='340' side='right' caption='[[1w36]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_V Exodeoxyribonuclease V], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.5 3.1.11.5] </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=1w36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w36 OCA], [http://pdbe.org/1w36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w36 RCSB], [http://www.ebi.ac.uk/pdbsum/1w36 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=1w36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w36 OCA], [http://pdbe.org/1w36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w36 RCSB], [http://www.ebi.ac.uk/pdbsum/1w36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w36 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w3/1w36_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w3/1w36_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1w36

From Proteopedia

Revision as of 07:50, 4 April 2018

RecBCD:DNA complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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