6rks: Difference between revisions

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'''Unreleased structure'''


The entry 6rks is ON HOLD until Paper Publication
==E. coli DNA Gyrase - DNA binding and cleavage domain in State 1 without TOPRIM insertion==
 
<StructureSection load='6rks' size='340' side='right'caption='[[6rks]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6rks]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RKS FirstGlance]. <br>
Description:  
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JHN:(3~{R})-3-[[4-(3,4-dihydro-2~{H}-pyrano[2,3-c]pyridin-6-ylmethylamino)piperidin-1-yl]methyl]-1,4,7-triazatricyclo[6.3.1.0^{4,12}]dodeca-6,8(12),9-triene-5,11-dione'>JHN</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isomerase Isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.6.2.3 5.6.2.3] </span></td></tr>
<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=6rks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rks OCA], [http://pdbe.org/6rks PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rks RCSB], [http://www.ebi.ac.uk/pdbsum/6rks PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rks ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GYRA_ECOLI GYRA_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:12051842</ref> <ref>PMID:18642932</ref> <ref>PMID:19965760</ref>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Isomerase]]
[[Category: Large Structures]]
[[Category: Broeck, A Vanden]]
[[Category: Lamour, V]]
[[Category: Complex]]
[[Category: Dna binding protein]]
[[Category: Dna gyrase]]
[[Category: Inhibitor]]

Revision as of 09:49, 6 November 2019

E. coli DNA Gyrase - DNA binding and cleavage domain in State 1 without TOPRIM insertionE. coli DNA Gyrase - DNA binding and cleavage domain in State 1 without TOPRIM insertion

Structural highlights

6rks is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Isomerase, with EC number 5.6.2.3
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GYRA_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. Hockings SC, Maxwell A. Identification of four GyrA residues involved in the DNA breakage-reunion reaction of DNA gyrase. J Mol Biol. 2002 Apr 26;318(2):351-9. PMID:12051842 doi:http://dx.doi.org/10.1016/S0022-2836(02)00048-7
  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. Edwards MJ, Flatman RH, Mitchenall LA, Stevenson CE, Le TB, Clarke TA, McKay AR, Fiedler HP, Buttner MJ, Lawson DM, Maxwell A. A crystal structure of the bifunctional antibiotic simocyclinone D8, bound to DNA gyrase. Science. 2009 Dec 4;326(5958):1415-8. PMID:19965760 doi:326/5958/1415

6rks, resolution 4.00Å

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