1ab4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ab4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ab4, resolution 2.8&Aring;" /> '''59KDA FRAGMENT OF GYR...)
Current revision (06:29, 7 February 2024) (edit) (undo)
 
(19 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ab4.gif|left|200px]]<br /><applet load="1ab4" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1ab4, resolution 2.8&Aring;" />
 
-
'''59KDA FRAGMENT OF GYRASE A FROM E. COLI'''<br />
 
-
==Overview==
+
==59KDA FRAGMENT OF GYRASE A FROM E. COLI==
-
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.
+
<StructureSection load='1ab4' size='340' side='right'caption='[[1ab4]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
 +
</table>
 +
== Function ==
 +
[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>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/1ab4_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1AB4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AB4 OCA].
+
*[[Gyrase 3D Structures|Gyrase 3D Structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9278055 9278055]
+
__TOC__
-
[[Category: DNA topoisomerase (ATP-hydrolyzing)]]
+
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Cabral, J.H.M.]]
+
[[Category: Cabral JHM]]
-
[[Category: Liddington, R.C.]]
+
[[Category: Liddington RC]]
-
[[Category: Maxwell, A.]]
+
[[Category: Maxwell A]]
-
[[Category: gyrase]]
+
-
[[Category: supercoiling dna]]
+
-
[[Category: topoisomerase ii]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:43:51 2007''
+

Current revision

59KDA FRAGMENT OF GYRASE A FROM E. COLI

PDB ID 1ab4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ab4"
Personal tools