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1qoj

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[[Image:1qoj.gif|left|200px]]
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{{STRUCTURE_1qoj| PDB=1qoj | SCENE= }}
{{STRUCTURE_1qoj| PDB=1qoj | SCENE= }}
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'''CRYSTAL STRUCTURE OF E.COLI UVRB C-TERMINAL DOMAIN, AND A MODEL FOR UVRB-UVRC INTERACTION.'''
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===CRYSTAL STRUCTURE OF E.COLI UVRB C-TERMINAL DOMAIN, AND A MODEL FOR UVRB-UVRC INTERACTION.===
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==Overview==
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A crystal structure of the C-terminal domain of Escherichia coli UvrB (UvrB') has been solved to 3.0 A resolution. The domain adopts a helix-loop-helix fold which is stabilised by the packing of hydrophobic side-chains between helices. From the UvrB' fold, a model for a domain of UvrC (UvrC') that has high sequence homology with UvrB' has been made. In the crystal, a dimerisation of UvrB domains is seen involving specific hydrophobic and salt bridge interactions between residues in and close to the loop region of the domain. It is proposed that a homologous mode of interaction may occur between UvrB and UvrC. This interaction is likely to be flexible, potentially spanning &gt; 50 A.
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(as it appears on PubMed at http://www.pubmed.gov), where 10631326 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10631326}}
==About this Structure==
==About this Structure==
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[[Category: Uvrb-c interaction]]
[[Category: Uvrb-c interaction]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:31:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:16:32 2008''

Revision as of 11:16, 28 July 2008

Template:STRUCTURE 1qoj

CRYSTAL STRUCTURE OF E.COLI UVRB C-TERMINAL DOMAIN, AND A MODEL FOR UVRB-UVRC INTERACTION.

Template:ABSTRACT PUBMED 10631326

About this Structure

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

Reference

Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction., Sohi M, Alexandrovich A, Moolenaar G, Visse R, Goosen N, Vernede X, Fontecilla-Camps JC, Champness J, Sanderson MR, FEBS Lett. 2000 Jan 14;465(2-3):161-4. PMID:10631326

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