3voa: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Staphylococcus aureus FtsZ 12-316 GDP-form== | |||
===Staphylococcus aureus | <StructureSection load='3voa' size='340' side='right' caption='[[3voa]], [[Resolution|resolution]] 1.73Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3voa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_mu50 Staphylococcus aureus subsp. aureus mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VOA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VOA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vo8|3vo8]], [[3vo9|3vo9]], [[3vob|3vob]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 Staphylococcus aureus subsp. aureus Mu50])</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=3voa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3voa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3voa RCSB], [http://www.ebi.ac.uk/pdbsum/3voa PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
FtsZ is a key molecule in bacterial cell division. In the presence of GTP, it polymerizes into tubulin-like protofilaments by head-to-tail association. Protofilaments of FtsZ seem to adopt a straight or a curved conformation in relation to the bound nucleotide. However, although several bacterial and archaeal FtsZ structures have been determined, all of the structures reported previously are considered to have a curved conformation. In this study, structures of FtsZ from Staphylococcus aureus (SaFtsZ) were determined in apo, GDP-bound and inhibitor-complex forms and it was found that SaFtsZ undergoes marked conformational changes. The accumulated evidence suggests that the GDP-bound structure has the features of the straight form. The structural change between the curved and straight forms shows intriguing similarity to the eukaryotic cytoskeletal protein tubulin. Furthermore, the structure of the apo form showed an unexpectedly large conformational change in the core region. FtsZ has also been recognized as a novel target for antibacterial drugs. The structure of the complex with the inhibitor PC190723, which has potent and selective antistaphylococcal activity, indicated that the inhibitor binds at the cleft between the two subdomains. | |||
Structural reorganization of the bacterial cell-division protein FtsZ from Staphylococcus aureus.,Matsui T, Yamane J, Mogi N, Yamaguchi H, Takemoto H, Yao M, Tanaka I Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1175-88. doi:, 10.1107/S0907444912022640. Epub 2012 Aug 18. PMID:22948918<ref>PMID:22948918</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Cell division protein Ftsz|Cell division protein Ftsz]] | *[[Cell division protein Ftsz|Cell division protein Ftsz]] | ||
*[[Tubulin|Tubulin]] | |||
== | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Staphylococcus aureus subsp. aureus mu50]] | [[Category: Staphylococcus aureus subsp. aureus mu50]] | ||
[[Category: Matsui, T | [[Category: Matsui, T]] | ||
[[Category: Mogi, N | [[Category: Mogi, N]] | ||
[[Category: Tanaka, I | [[Category: Tanaka, I]] | ||
[[Category: Yamane, J | [[Category: Yamane, J]] | ||
[[Category: Yao, M | [[Category: Yao, M]] | ||
[[Category: Cell cycle]] | [[Category: Cell cycle]] | ||
[[Category: Cell division]] | [[Category: Cell division]] | ||
Revision as of 12:27, 4 January 2015
Staphylococcus aureus FtsZ 12-316 GDP-formStaphylococcus aureus FtsZ 12-316 GDP-form
Structural highlights
Publication Abstract from PubMedFtsZ is a key molecule in bacterial cell division. In the presence of GTP, it polymerizes into tubulin-like protofilaments by head-to-tail association. Protofilaments of FtsZ seem to adopt a straight or a curved conformation in relation to the bound nucleotide. However, although several bacterial and archaeal FtsZ structures have been determined, all of the structures reported previously are considered to have a curved conformation. In this study, structures of FtsZ from Staphylococcus aureus (SaFtsZ) were determined in apo, GDP-bound and inhibitor-complex forms and it was found that SaFtsZ undergoes marked conformational changes. The accumulated evidence suggests that the GDP-bound structure has the features of the straight form. The structural change between the curved and straight forms shows intriguing similarity to the eukaryotic cytoskeletal protein tubulin. Furthermore, the structure of the apo form showed an unexpectedly large conformational change in the core region. FtsZ has also been recognized as a novel target for antibacterial drugs. The structure of the complex with the inhibitor PC190723, which has potent and selective antistaphylococcal activity, indicated that the inhibitor binds at the cleft between the two subdomains. Structural reorganization of the bacterial cell-division protein FtsZ from Staphylococcus aureus.,Matsui T, Yamane J, Mogi N, Yamaguchi H, Takemoto H, Yao M, Tanaka I Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1175-88. doi:, 10.1107/S0907444912022640. Epub 2012 Aug 18. PMID:22948918[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||