1w36

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[[Image:1w36.gif|left|200px]]
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{{STRUCTURE_1w36| PDB=1w36 | SCENE= }}
{{STRUCTURE_1w36| PDB=1w36 | SCENE= }}
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'''RECBCD:DNA COMPLEX'''
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===RECBCD:DNA COMPLEX===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15538360 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15538360}}
==About this Structure==
==About this Structure==
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[[Category: Nuclease]]
[[Category: Nuclease]]
[[Category: Recombination]]
[[Category: Recombination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:05:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:49:14 2008''

Revision as of 17:49, 28 July 2008

Template:STRUCTURE 1w36

RECBCD:DNA COMPLEX

Template:ABSTRACT PUBMED 15538360

About this Structure

1W36 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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