1lrr

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Revision as of 21:41, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1lrr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lrr, resolution 2.65Å" /> '''CRYSTAL STRUCTURE OF...)
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File:1lrr.gif


1lrr, resolution 2.65Å

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CRYSTAL STRUCTURE OF E. COLI SEQA COMPLEXED WITH HEMIMETHYLATED DNA

OverviewOverview

The SeqA protein binds clusters of fully methylated or hemimethylated GATC, sequences at oriC and negatively modulates the initiation of DNA, replication. We find that SeqA can be proteolytically cleaved into an, N-terminal multimerization and a C-terminal DNA-binding domain and have, determined the crystal structure of the C-terminal domain in complex with, a hemimethylated GATC site. SeqA makes direct hydrogen bonds and van der, Waals contacts with the hemimethylated A-T base pair in addition to, interactions with the surrounding bases and DNA backbone. The tetrameric, protein-DNA complex found in the crystal suggests that SeqA binds multiple, GATC sites on separate DNA duplexes, altering the overall DNA topology and, sequestering oriC from replication initiation.

About this StructureAbout this Structure

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

ReferenceReference

Insights into negative modulation of E. coli replication initiation from the structure of SeqA-hemimethylated DNA complex., Guarne A, Zhao Q, Ghirlando R, Yang W, Nat Struct Biol. 2002 Nov;9(11):839-43. PMID:12379844

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