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6umk

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Structure of E. coli FtsZ(L178E)-GDP complex

Structural highlights

6umk is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.35Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]

Publication Abstract from PubMed

Bacterial cytokinesis is mediated by the Z-ring, which is formed by the prokaryotic tubulin homolog FtsZ. Recent data indicate that the Z-ring is composed of small patches of FtsZ protofilaments that travel around the bacterial cell by treadmilling. Treadmilling involves a switch from a relaxed (R) state, favored for monomers, to a tense (T) conformation, which is favored upon association into filaments. The R conformation has been observed in numerous monomeric FtsZ crystal structures and the T conformation in Staphylococcus aureus FtsZ crystallized as assembled filaments. However, while Escherichia coli has served as a main model system for the study of the Z-ring and the associated divisome, a structure has not yet been reported for E. coli FtsZ. To address this gap, structures were determined of the E. coli FtsZ mutant FtsZ(L178E) with GDP and GTP bound to 1.35 and 1.40 A resolution, respectively. The E. coli FtsZ(L178E) structures both crystallized as straight filaments with subunits in the R conformation. These high-resolution structures can be employed to facilitate experimental cell-division studies and their interpretation in E. coli.

High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP.,Schumacher MA, Ohashi T, Corbin L, Erickson HP Acta Crystallogr F Struct Biol Commun. 2020 Feb 1;76(Pt 2):94-102. doi:, 10.1107/S2053230X20001132. Epub 2020 Feb 5. PMID:32039891^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schumacher MA, Ohashi T, Corbin L, Erickson HP. High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP. Acta Crystallogr F Struct Biol Commun. 2020 Feb 1;76(Pt 2):94-102. doi:, 10.1107/S2053230X20001132. Epub 2020 Feb 5. PMID:32039891 doi:http://dx.doi.org/10.1107/S2053230X20001132

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6umk"

Categories: Escherichia coli | Large Structures | Schumacher MA

@@ Line 3: / Line 3: @@
 <StructureSection load='6umk' size='340' side='right'caption='[[6umk]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6umk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UMK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6UMK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6umk]] 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=6UMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UMK FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsZ, D4U49_01465, DNQ92_00675 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+<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>
-<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=6umk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6umk OCA], [http://pdbe.org/6umk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6umk RCSB], [http://www.ebi.ac.uk/pdbsum/6umk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6umk ProSAT]</span></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=6umk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6umk OCA], [https://pdbe.org/6umk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6umk RCSB], [https://www.ebi.ac.uk/pdbsum/6umk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6umk ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A0A3T9KGL2_ECOLX A0A3T9KGL2_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]
+[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]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 6umk" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cell division protein 3D structures|Cell division protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Schumacher, M A]]
+[[Category: Schumacher MA]]
-[[Category: Cell cycle]]
-[[Category: Closed state]]
-[[Category: E. coli]]
-[[Category: Ftsz]]
-[[Category: Model system]]

6umk

From Proteopedia

Current revision

Structure of E. coli FtsZ(L178E)-GDP complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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