1rlu

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[[Image:1rlu.gif|left|200px]]<br /><applet load="1rlu" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rlu, resolution 2.08&Aring;" />
 
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'''Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S'''<br />
 
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==Overview==
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==Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S==
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<StructureSection load='1rlu' size='340' side='right'caption='[[1rlu]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rlu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RLU FirstGlance]. <br>
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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]] 2.08&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene></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=1rlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rlu OCA], [https://pdbe.org/1rlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rlu RCSB], [https://www.ebi.ac.uk/pdbsum/1rlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rlu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FTSZ_MYCTU FTSZ_MYCTU] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells (By similarity). Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909]
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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/rl/1rlu_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=1rlu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
We report three crystal structures of the Mycobacterium tuberculosis cell division protein FtsZ, as the citrate, GDP, and GTPgammaS complexes, determined at 1.89, 2.60, and 2.08A resolution. MtbFtsZ crystallized as a tight, laterally oriented dimer distinct from the longitudinal polymer observed for alphabeta-tubulin. Mutational data on Escherichia coli FtsZ suggest that this dimer interface is important for proper protofilament and "Z-ring" assembly and function. An alpha-to-beta secondary structure conformational switch at the dimer interface is spatially analogous to, and has many of the hallmarks of, the Switch I conformational changes exhibited by G-proteins upon activation. The presence of a gamma-phosphate in the FtsZ active site modulates the conformation of the "tubulin" loop T3 (spatially analogous to the G-protein Switch II); T3 switching upon gamma-phosphate ligation is directly coupled to the alpha-to-beta switch by steric overlap. The dual conformational switches observed here for the first time in an FtsZ link GTP binding and hydrolysis to FtsZ (and tubulin) lateral assembly and Z-ring contraction, and they are suggestive of an underappreciated functional analogy between FtsZ, tubulin and G-proteins.
We report three crystal structures of the Mycobacterium tuberculosis cell division protein FtsZ, as the citrate, GDP, and GTPgammaS complexes, determined at 1.89, 2.60, and 2.08A resolution. MtbFtsZ crystallized as a tight, laterally oriented dimer distinct from the longitudinal polymer observed for alphabeta-tubulin. Mutational data on Escherichia coli FtsZ suggest that this dimer interface is important for proper protofilament and "Z-ring" assembly and function. An alpha-to-beta secondary structure conformational switch at the dimer interface is spatially analogous to, and has many of the hallmarks of, the Switch I conformational changes exhibited by G-proteins upon activation. The presence of a gamma-phosphate in the FtsZ active site modulates the conformation of the "tubulin" loop T3 (spatially analogous to the G-protein Switch II); T3 switching upon gamma-phosphate ligation is directly coupled to the alpha-to-beta switch by steric overlap. The dual conformational switches observed here for the first time in an FtsZ link GTP binding and hydrolysis to FtsZ (and tubulin) lateral assembly and Z-ring contraction, and they are suggestive of an underappreciated functional analogy between FtsZ, tubulin and G-proteins.
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==About this Structure==
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Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches.,Leung AK, Lucile White E, Ross LJ, Reynolds RC, DeVito JA, Borhani DW J Mol Biol. 2004 Sep 17;342(3):953-70. PMID:15342249<ref>PMID:15342249</ref>
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1RLU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=GSP:'>GSP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLU OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches., Leung AK, Lucile White E, Ross LJ, Reynolds RC, DeVito JA, Borhani DW, J Mol Biol. 2004 Sep 17;342(3):953-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15342249 15342249]
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</div>
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[[Category: Mycobacterium tuberculosis]]
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<div class="pdbe-citations 1rlu" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Borhani, D W.]]
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[[Category: DeVito, J A.]]
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[[Category: Leung, A K.W.]]
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[[Category: Reynolds, R C.]]
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[[Category: Ross, L J.]]
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[[Category: White, E L.]]
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[[Category: GOL]]
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[[Category: GSP]]
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[[Category: cell cycle]]
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[[Category: gtpase]]
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[[Category: tubulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:18 2008''
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==See Also==
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*[[Cell division protein 3D structures|Cell division protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Borhani DW]]
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[[Category: DeVito JA]]
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[[Category: Leung AKW]]
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[[Category: Reynolds RC]]
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[[Category: Ross LJ]]
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[[Category: White EL]]

Current revision

Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S

PDB ID 1rlu

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