4tma: Difference between revisions

No edit summary
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Crystal structure of gyrase bound to its inhibitor YacG==
==Crystal structure of gyrase bound to its inhibitor YacG==
<StructureSection load='4tma' size='340' side='right' caption='[[4tma]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='4tma' size='340' side='right'caption='[[4tma]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4tma]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TMA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TMA FirstGlance]. <br>
<table><tr><td colspan='2'>[[4tma]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MC4100 Escherichia coli str. K-12 substr. MC4100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TMA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.3&#8491;</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4tma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tma OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tma RCSB], [http://www.ebi.ac.uk/pdbsum/4tma PDBsum]</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=4tma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tma OCA], [https://pdbe.org/4tma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tma RCSB], [https://www.ebi.ac.uk/pdbsum/4tma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tma ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/U6NB78_ECOLI U6NB78_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 (By similarity).[HAMAP-Rule:MF_01897] [[http://www.uniprot.org/uniprot/YACG_ECOLI YACG_ECOLI]] Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.<ref>PMID:18586829</ref> [[http://www.uniprot.org/uniprot/U6NGU8_ECOLI U6NGU8_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 (By similarity).[HAMAP-Rule:MF_01898]
[https://www.uniprot.org/uniprot/YACG_ECOLI YACG_ECOLI] Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.<ref>PMID:18586829</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 17: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4tma" style="background-color:#fffaf0;"></div>
==See Also==
*[[Gyrase 3D Structures|Gyrase 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Berger, J M]]
[[Category: Escherichia coli K-12]]
[[Category: Hershey, D M]]
[[Category: Escherichia coli str. K-12 substr. MC4100]]
[[Category: Lyubimov, A Y]]
[[Category: Large Structures]]
[[Category: Schoeffler, A J]]
[[Category: Berger JM]]
[[Category: Vos, S M]]
[[Category: Hershey DM]]
[[Category: Duf329]]
[[Category: Lyubimov AY]]
[[Category: Isomerase]]
[[Category: Schoeffler AJ]]
[[Category: Isomerase-isomerase inhibitor complex]]
[[Category: Vos SM]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA