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1wud

From Proteopedia

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E. coli RecQ HRDC domain

Structural highlights

1wud is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RECQ_ECOLI Involved in the RecF recombination pathway; its gene expression is under the regulation of the SOS system. It is a DNA helicase.

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

RecQ DNA helicases are multidomain enzymes that play pivotal roles in genome maintenance pathways. While the ATPase and helicase activities of these enzymes can be attributed to the conserved catalytic core domain, the role of the Helicase-and-RNase-D-C-terminal (HRDC) domain in RecQ function has yet to be elucidated. Here, we report the crystal structure of the E. coli RecQ HRDC domain, revealing a globular fold that resembles known DNA binding domains. We show that this domain preferentially binds single-stranded DNA and identify its DNA binding surface. HRDC domain mutations in full-length RecQ lead to surprising differences in its structure-specific DNA binding properties. These data support a model in which naturally occurring variations in DNA binding residues among diverse RecQ homologs serve to target these enzymes to distinct substrates and provide insight into a mechanism whereby RecQ enzymes have evolved distinct functions in organisms that encode multiple recQ genes.

Conferring substrate specificity to DNA helicases: role of the RecQ HRDC domain.,Bernstein DA, Keck JL Structure. 2005 Aug;13(8):1173-82. PMID:16084389^[1]

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

References

↑ Bernstein DA, Keck JL. Conferring substrate specificity to DNA helicases: role of the RecQ HRDC domain. Structure. 2005 Aug;13(8):1173-82. PMID:16084389 doi:http://dx.doi.org/10.1016/j.str.2005.04.018

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/1wud"

Categories: Escherichia coli | Large Structures | Bernstein DA | Keck JL

@@ Line 3: / Line 3: @@
 <StructureSection load='1wud' size='340' side='right'caption='[[1wud]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wud]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WUD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wud]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WUD FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wud OCA], [https://pdbe.org/1wud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wud RCSB], [https://www.ebi.ac.uk/pdbsum/1wud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wud ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/RECQ_ECOLI RECQ_ECOLI]] Involved in the RecF recombination pathway; its gene expression is under the regulation of the SOS system. It is a DNA helicase.
+[https://www.uniprot.org/uniprot/RECQ_ECOLI RECQ_ECOLI] Involved in the RecF recombination pathway; its gene expression is under the regulation of the SOS system. It is a DNA helicase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Bernstein, D A]]
+[[Category: Bernstein DA]]
-[[Category: Keck, J L]]
+[[Category: Keck JL]]
-[[Category: Dna-binding domain]]
-[[Category: Helicase]]
-[[Category: Hrdc]]
-[[Category: Hydrolase]]
-[[Category: Recq]]

1wud

From Proteopedia

Current revision

E. coli RecQ HRDC domain

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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