4wud: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wud]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WUD FirstGlance]. <br> | <table><tr><td colspan='2'>[[4wud]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WUD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wud OCA], [https://pdbe.org/4wud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wud RCSB], [https://www.ebi.ac.uk/pdbsum/4wud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wud ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wud OCA], [https://pdbe.org/4wud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wud RCSB], [https://www.ebi.ac.uk/pdbsum/4wud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wud ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 13:44, 10 January 2024
N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from no salt conditionN-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit grown from no salt condition
Structural highlights
FunctionGYRB_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] Publication Abstract from PubMedFour new crystal structures of the ATPase domain of the GyrB subunit of Escherichia coli DNA gyrase have been determined. One of these, solved in the presence of K(+), is the highest resolution structure reported so far for this domain and, in conjunction with the three other structures, reveals new insights into the function of this domain. Evidence is provided for the existence of two monovalent cation-binding sites: site 1, which preferentially binds a K(+) ion that interacts directly with the alpha-phosphate of ATP, and site 2, which preferentially binds an Na(+) ion and the functional significance of which is not clear. The crystallographic data are corroborated by ATPase data, and the structures are compared with those of homologues to investigate the broader conservation of these sites. The role of monovalent cations in the ATPase reaction of DNA gyrase.,Hearnshaw SJ, Chung TT, Stevenson CE, Maxwell A, Lawson DM Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):996-1005. doi:, 10.1107/S1399004715002916. Epub 2015 Mar 27. PMID:25849408[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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