|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Mycobacterium tuberculosis gyrase type IIA topoisomerase C-terminal domain at 1.4 A resolution== | | ==Mycobacterium tuberculosis gyrase type IIA topoisomerase C-terminal domain at 1.4 A resolution== |
| - | <StructureSection load='4g3n' size='340' side='right' caption='[[4g3n]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='4g3n' size='340' side='right'caption='[[4g3n]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4g3n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G3N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G3N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4g3n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G3N FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gyrA, MT0006, mtct10h4.04, MTCY10H4.04, Rv0006, rv006 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr> | + | </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=4g3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g3n OCA], [https://pdbe.org/4g3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g3n RCSB], [https://www.ebi.ac.uk/pdbsum/4g3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g3n ProSAT]</span></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='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=4g3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g3n OCA], [http://pdbe.org/4g3n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g3n RCSB], [http://www.ebi.ac.uk/pdbsum/4g3n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g3n ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GYRA_MYCTU GYRA_MYCTU]] 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. | + | [https://www.uniprot.org/uniprot/GYRA_MYCTU GYRA_MYCTU] 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 19: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Gyrase|Gyrase]] | + | *[[Gyrase 3D Structures|Gyrase 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Myctu]] | + | [[Category: Large Structures]] |
| - | [[Category: Aubry, A]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Darmon, A]] | + | [[Category: Aubry A]] |
| - | [[Category: Mayer, C]] | + | [[Category: Darmon A]] |
| - | [[Category: Petrella, S]] | + | [[Category: Mayer C]] |
| - | [[Category: Piton, J]] | + | [[Category: Petrella S]] |
| - | [[Category: Beta-propeller]]
| + | [[Category: Piton J]] |
| - | [[Category: Dna gyrase c-terminal domain]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Topoisomerase type iia]]
| + | |
| Structural highlights
Function
GYRA_MYCTU 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.
Publication Abstract from PubMed
In contrast to most bacteria which possess two type II topoisomerases (Topo IV and DNA gyrase), Mycobacterium tuberculosis possesses only one, DNA gyrase, which is functionally a hybrid enzyme. Functional differences between the two type IIA topoisomerases are thought to be specified by a C-terminal DNA binding domain (CTD) which controls DNA recognition. To explore the molecular mechanism responsible for the hybrid functions of the M. tuberculosis DNA gyrase, we conducted a series of sequence analyses and structural and biochemical experiments with the isolated GyrA CTD and the holoenzyme. While the CTD displayed a global structure similar to that of bona fide GyrA and ParC paralogs, it harbors a second key motif similar in all respects to that of the conserved GyrA-box sequence motif. Biochemical assays showed that the GyrA-box is responsible for DNA supercoiling, whereas the second GyrA-box-like motif (GyrA-box-l) is responsible for the enhanced decatenation activity suggesting that the mechanistic originality of M. tuberculosis DNA gyrase depends largely on the particular DNA path around the CTD allowed for by the presence of GyrA-box-l. Our results provide also, through phylogenetic exploration of the entire Corynebacterineae suborder, new and broader insight into the functional diversity of bacterial type IIA topoisomerases.
The Mycobacterium tuberculosis DNA gyrase possesses two functional GyrA-boxes.,Bouige A, Darmon A, Piton J, Roue M, Petrella S, Capton E, Forterre P, Aubry A, Mayer C Biochem J. 2013 Jul 22. PMID:23869946[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bouige A, Darmon A, Piton J, Roue M, Petrella S, Capton E, Forterre P, Aubry A, Mayer C. The Mycobacterium tuberculosis DNA gyrase possesses two functional GyrA-boxes. Biochem J. 2013 Jul 22. PMID:23869946 doi:10.1042/BJ20130430
|
