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4kfg

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'''Unreleased structure'''
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{{STRUCTURE_4kfg| PDB=4kfg | SCENE= }}
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===The DNA Gyrase B ATP binding domain of Escherichia coli in complex with a small molecule inhibitor.===
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The entry 4kfg is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/GYRB_ECOLI GYRB_ECOLI]] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings.<ref>PMID:12051843</ref> <ref>PMID:18642932</ref> <ref>PMID:20675723</ref>
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Authors: Bensen, D.C., Akers-Rodriguez, S., Lam, T., Tari, L.W.
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==About this Structure==
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[[4kfg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KFG OCA].
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Description: The DNA Gyrase B ATP binding domain of Escherichia coli in complex with a small molecule inhibitor.
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Akers-Rodriguez, S.]]
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[[Category: Bensen, D C.]]
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[[Category: Lam, T.]]
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[[Category: Tari, L W.]]
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[[Category: Atp-binding]]
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[[Category: Atp-binding domain]]
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[[Category: Isomerase-isomerase inhibitor complex]]
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[[Category: Nucleotide-binding]]
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[[Category: Topoisomerase]]

Revision as of 08:23, 15 January 2014

Template:STRUCTURE 4kfg

Contents

The DNA Gyrase B ATP binding domain of Escherichia coli in complex with a small molecule inhibitor.

Function

[GYRB_ECOLI] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings.[1] [2] [3]

About this Structure

4kfg is a 2 chain structure. Full crystallographic information is available from OCA.

Reference

  1. ↑ Noble CG, Maxwell A. The role of GyrB in the DNA cleavage-religation reaction of DNA gyrase: a proposed two metal-ion mechanism. J Mol Biol. 2002 Apr 26;318(2):361-71. PMID:12051843 doi:http://dx.doi.org/10.1016/S0022-2836(02)00049-9
  2. ↑ Sissi C, Chemello A, Vazquez E, Mitchenall LA, Maxwell A, Palumbo M. DNA gyrase requires DNA for effective two-site coordination of divalent metal ions: further insight into the mechanism of enzyme action. Biochemistry. 2008 Aug 19;47(33):8538-45. doi: 10.1021/bi800480j. Epub 2008 Jul, 22. PMID:18642932 doi:http://dx.doi.org/10.1021/bi800480j
  3. ↑ Schoeffler AJ, May AP, Berger JM. A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function. Nucleic Acids Res. 2010 Jul 31. PMID:20675723 doi:10.1093/nar/gkq665

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