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1w5f

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Revision as of 18:42, 24 January 2018

FtsZ, T7 mutated, domain swapped (T. maritima)

Structural highlights

1w5f is a 2 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1fsz, 1w58, 1w59, 1w5a, 1w5b, 1w5e
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FTSZ_THEMA] 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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure essential for bacterial cell division. We have used refolded FtsZ to crystallize a tubulin-like protofilament. The N- and C-terminal domains of two consecutive subunits in the filament assemble to form the GTPase site, with the C-terminal domain providing water-polarizing residues. A domain-swapped structure of FtsZ and biochemical data on purified N- and C-terminal domains show that they are independent. This leads to a model of how FtsZ and tubulin polymerization evolved by fusing two domains. In polymerized tubulin, the nucleotide-binding pocket is occluded, which leads to nucleotide exchange being the rate-limiting step and to dynamic instability. In our FtsZ filament structure the nucleotide is exchangeable, explaining why, in this filament, nucleotide hydrolysis is the rate-limiting step during FtsZ polymerization. Furthermore, crystal structures of FtsZ in different nucleotide states reveal notably few differences.

Structural insights into FtsZ protofilament formation.,Oliva MA, Cordell SC, Lowe J Nat Struct Mol Biol. 2004 Dec;11(12):1243-50. Epub 2004 Nov 21. PMID:15558053^[2]

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

References

↑ Lu C, Stricker J, Erickson HP. FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima--quantitation, GTP hydrolysis, and assembly. Cell Motil Cytoskeleton. 1998;40(1):71-86. PMID:9605973 doi:<71::AID-CM7>3.0.CO;2-I http://dx.doi.org/10.1002/(SICI)1097-0169(1998)40:1<71::AID-CM7>3.0.CO;2-I
↑ Oliva MA, Cordell SC, Lowe J. Structural insights into FtsZ protofilament formation. Nat Struct Mol Biol. 2004 Dec;11(12):1243-50. Epub 2004 Nov 21. PMID:15558053 doi:10.1038/nsmb855

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w5f"

@@ Line 1: / Line 1: @@
-==FTSZ, T7 MUTATED, DOMAIN SWAPPED (T. MARITIMA)==
+==FtsZ, T7 mutated, domain swapped (T. maritima)==
 <StructureSection load='1w5f' size='340' side='right' caption='[[1w5f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fsz|1fsz]], [[1w58|1w58]], [[1w59|1w59]], [[1w5a|1w5a]], [[1w5b|1w5b]], [[1w5e|1w5e]]</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=1w5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w5f OCA], [http://pdbe.org/1w5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w5f RCSB], [http://www.ebi.ac.uk/pdbsum/1w5f PDBsum]</span></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=1w5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w5f OCA], [http://pdbe.org/1w5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w5f RCSB], [http://www.ebi.ac.uk/pdbsum/1w5f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w5f ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w5/1w5f_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w5/1w5f_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1w5f ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1w5f" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Cell division protein Ftsz|Cell division protein Ftsz]]
-*[[Tubulin|Tubulin]]
 == References ==
 <references/>

1w5f

From Proteopedia

Revision as of 18:42, 24 January 2018

FtsZ, T7 mutated, domain swapped (T. maritima)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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