1wud: Difference between revisions

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[[Image:1wud.gif|left|200px]]
{{Seed}}
[[Image:1wud.png|left|200px]]


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{{STRUCTURE_1wud|  PDB=1wud  |  SCENE=  }}  
{{STRUCTURE_1wud|  PDB=1wud  |  SCENE=  }}  


'''E. coli RecQ HRDC domain'''
===E. coli RecQ HRDC domain===




==Overview==
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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.
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{{ABSTRACT_PUBMED_16084389}}


==About this Structure==
==About this Structure==
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[[Category: Hrdc]]
[[Category: Hrdc]]
[[Category: Recq]]
[[Category: Recq]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:08:46 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:30:28 2008''

Revision as of 23:30, 27 July 2008

File:1wud.png

Template:STRUCTURE 1wud

E. coli RecQ HRDC domain

Template:ABSTRACT PUBMED 16084389

About this Structure

1WUD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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