1wud
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(New page: 200px<br /><applet load="1wud" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wud, resolution 2.20Å" /> '''E. coli RecQ HRDC do...)
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Revision as of 03:33, 21 November 2007
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E. coli RecQ HRDC domain
Overview
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.
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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