1ab4

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[[Image:1ab4.gif|left|200px]]
 
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==59KDA FRAGMENT OF GYRASE A FROM E. COLI==
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The line below this paragraph, containing "STRUCTURE_1ab4", creates the "Structure Box" on the page.
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<StructureSection load='1ab4' size='340' side='right'caption='[[1ab4]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ab4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AB4 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ab4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ab4 OCA], [https://pdbe.org/1ab4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ab4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ab4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ab4 ProSAT]</span></td></tr>
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{{STRUCTURE_1ab4| PDB=1ab4 | SCENE= }}
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</table>
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== Function ==
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[https://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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/1ab4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ab4 ConSurf].
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<div style="clear:both"></div>
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'''59KDA FRAGMENT OF GYRASE A FROM E. COLI'''
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==See Also==
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*[[Gyrase 3D Structures|Gyrase 3D Structures]]
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== References ==
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==Overview==
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<references/>
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DNA gyrase is a type II DNA topoisomerase from bacteria that introduces supercoils into DNA. It catalyses the breakage of a DNA duplex (the G segment), the passage of another segment (the T segment) through the break, and then the reunification of the break. This activity involves the opening and dosing of a series of molecular 'gates' which is coupled to ATP hydrolysis. Here we present the crystal structure of the 'breakage-reunion' domain of the gyrase at 2.8 A resolution. Comparison of the structure of this 59K (relative molecular mass, 59,000) domain with that of a 92K fragment of yeast topoisomerase II reveals a very different quaternary organization, and we propose that the two structures represent two principal conformations that participate in the enzymatic pathway. The gyrase structure reveals a new dimer contact with a grooved concave surface for binding the G segment and a cluster of conserved charged residues surrounding the active-site tyrosines. It also shows how breakage of the G segment can occur and, together with the topoisomerase II structure, suggests a pathway by which the T segment can be released through the second gate of the enzyme. Mutations that confer resistance to the quinolone antibacterial agents cluster at the new dimer interface, indicating how these drugs might interact with the gyrase-DNA complex.
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__TOC__
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</StructureSection>
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==About this Structure==
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1AB4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AB4 OCA].
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==Reference==
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Crystal structure of the breakage-reunion domain of DNA gyrase., Morais Cabral JH, Jackson AP, Smith CV, Shikotra N, Maxwell A, Liddington RC, Nature. 1997 Aug 28;388(6645):903-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9278055 9278055]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cabral, J H.M.]]
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[[Category: Cabral JHM]]
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[[Category: Liddington, R C.]]
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[[Category: Liddington RC]]
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[[Category: Maxwell, A.]]
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[[Category: Maxwell A]]
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[[Category: Gyrase]]
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[[Category: Supercoiling dna]]
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[[Category: Topoisomerase ii]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:03:54 2008''
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Current revision

59KDA FRAGMENT OF GYRASE A FROM E. COLI

PDB ID 1ab4

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