6ll6

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Current revision (10:46, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6ll6' size='340' side='right'caption='[[6ll6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='6ll6' size='340' side='right'caption='[[6ll6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ll6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6LL6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ll6]] 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=6LL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LL6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
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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]] 2.5&#8491;</td></tr>
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<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=6ll6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ll6 OCA], [http://pdbe.org/6ll6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ll6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ll6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ll6 ProSAT]</span></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=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=6ll6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ll6 OCA], [https://pdbe.org/6ll6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ll6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ll6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ll6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/A0A2W6PFK5_ECOLX A0A2W6PFK5_ECOLX]] 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. Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909][RuleBase:RU000631]
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[https://www.uniprot.org/uniprot/FTSZ_ECOLI FTSZ_ECOLI] 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. Binds GTP and shows GTPase activity. Polymerization and bundle formation is enhanced by CbeA.[HAMAP-Rule:MF_00909]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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FtsZ, a tubulin-like GTPase, is essential for bacterial cell division. In the presence of GTP, FtsZ polymerizes into filamentous structures, which are key to generating force in cell division. However, the structural basis for the molecular mechanism underlying FtsZ function remains to be elucidated. In this study, crystal structures of the enzymatic domains of FtsZ from Klebsiella pneumoniae (KpFtsZ) and Escherichia coli (EcFtsZ) were determined at 1.75 and 2.50 A resolution, respectively. Both FtsZs form straight protofilaments in the crystals, and the two structures adopted relaxed (R) conformations. The T3 loop, which is involved in GTP/GDP binding and FtsZ assembly/disassembly, adopted a unique open conformation in KpFtsZ, while the T3 loop of EcFtsZ was partially disordered. The crystal structure of EcFtsZ can explain the results from previous functional analyses using EcFtsZ mutants.
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Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli.,Yoshizawa T, Fujita J, Terakado H, Ozawa M, Kuroda N, Tanaka SI, Uehara R, Matsumura H Acta Crystallogr F Struct Biol Commun. 2020 Feb 1;76(Pt 2):86-93. doi:, 10.1107/S2053230X2000076X. Epub 2020 Feb 5. PMID:32039890<ref>PMID:32039890</ref>
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==See Also==
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*[[Cell division protein 3D structures|Cell division protein 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ll6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fujita, J]]
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[[Category: Fujita J]]
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[[Category: Kuroda, N]]
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[[Category: Kuroda N]]
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[[Category: Matsumura, H]]
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[[Category: Matsumura H]]
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[[Category: Ozawa, M]]
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[[Category: Ozawa M]]
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[[Category: Tanaka, S]]
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[[Category: Tanaka S]]
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[[Category: Terakada, H]]
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[[Category: Terakada H]]
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[[Category: Uehara, R]]
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[[Category: Uehara R]]
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[[Category: Yoshizawa, T]]
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[[Category: Yoshizawa T]]
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[[Category: Cell cycle]]
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[[Category: Cell division]]
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[[Category: Escherichia coli]]
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Current revision

Crsyal structure of EcFtsZ (residues 11-316)

PDB ID 6ll6

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