4xtj: Difference between revisions

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'''Unreleased structure'''
==N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from 100 mM KCl plus 100 mM NaCl condition==
 
<StructureSection load='4xtj' size='340' side='right' caption='[[4xtj]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
The entry 4xtj is ON HOLD
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4xtj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XTJ FirstGlance]. <br>
Authors: Hearnshaw, S.J., Chung, T.T., Stevenson, C.E.M., Maxwell, A., Lawson, D.M.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
 
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] </span></td></tr>
Description: N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from 100 mM KCl plus 100 mM NaCl condition
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xtj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xtj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xtj RCSB], [http://www.ebi.ac.uk/pdbsum/4xtj PDBsum]</span></td></tr>
[[Category: Unreleased Structures]]
</table>
[[Category: Chung, T.T]]
== Function ==
[[Category: Stevenson, C.E.M]]
[[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> 
[[Category: Hearnshaw, S.J]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chung, T T]]
[[Category: Hearnshaw, S J]]
[[Category: Lawson, D M]]
[[Category: Maxwell, A]]
[[Category: Maxwell, A]]
[[Category: Lawson, D.M]]
[[Category: Stevenson, C E.M]]
[[Category: Atpase activity]]
[[Category: Atpase domain]]
[[Category: Dna gyrase]]
[[Category: Ghkl superfamily]]
[[Category: Isomerase]]
[[Category: Monovalent cation]]

Revision as of 14:18, 8 April 2015

N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from 100 mM KCl plus 100 mM NaCl conditionN-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from 100 mM KCl plus 100 mM NaCl condition

Structural highlights

4xtj is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Activity:DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3
Resources:FirstGlance, OCA, RCSB, PDBsum

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]

References

  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

4xtj, resolution 1.92Å

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