4b45: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='4b45' size='340' side='right'caption='[[4b45]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4b45' size='340' side='right'caption='[[4b45]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4b45]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29605 Atcc 29605]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B45 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B45 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4b45]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloferax_volcanii Haloferax volcanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B45 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</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]] 2.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b46|4b46]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</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=4b45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b45 OCA], [http://pdbe.org/4b45 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b45 RCSB], [http://www.ebi.ac.uk/pdbsum/4b45 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b45 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=4b45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b45 OCA], [https://pdbe.org/4b45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b45 RCSB], [https://www.ebi.ac.uk/pdbsum/4b45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b45 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/CETZ2_HALVD CETZ2_HALVD] Involved in cell shape control.[HAMAP-Rule:MF_01946]<ref>PMID:25533961</ref>  
Tubulin is a major component of the eukaryotic cytoskeleton, controlling cell shape, structure and dynamics, whereas its bacterial homologue FtsZ establishes the cytokinetic ring that constricts during cell division. How such different roles of tubulin and FtsZ evolved is unknown. Studying Archaea may provide clues as these organisms share characteristics with Eukarya and Bacteria. Here we report the structure and function of proteins from a distinct family related to tubulin and FtsZ, named CetZ, which co-exists with FtsZ in many archaea. CetZ X-ray crystal structures showed the FtsZ/tubulin superfamily fold, and one crystal form contained sheets of protofilaments, suggesting a structural role. However, inactivation of CetZ proteins in Haloferax volcanii did not affect cell division. Instead, CetZ1 was required for differentiation of the irregular plate-shaped cells into a rod-shaped cell type that was essential for normal swimming motility. CetZ1 formed dynamic cytoskeletal structures in vivo, relating to its capacity to remodel the cell envelope and direct rod formation. CetZ2 was also implicated in H. volcanii cell shape control. Our findings expand the known roles of the FtsZ/tubulin superfamily to include archaeal cell shape dynamics, suggesting that a cytoskeletal role might predate eukaryotic cell evolution, and they support the premise that a major function of the microbial rod shape is to facilitate swimming.
 
CetZ tubulin-like proteins control archaeal cell shape.,Duggin IG, Aylett CH, Walsh JC, Michie KA, Wang Q, Turnbull L, Dawson EM, Harry EJ, Whitchurch CB, Amos LA, Lowe J Nature. 2014 Dec 22. doi: 10.1038/nature13983. PMID:25533961<ref>PMID:25533961</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4b45" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cell division protein|Cell division protein]]
*[[Cell division protein 3D structures|Cell division protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 29605]]
[[Category: Haloferax volcanii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Aylett, C H.S]]
[[Category: Aylett CHS]]
[[Category: Duggin, I G]]
[[Category: Duggin IG]]
[[Category: Lowe, J]]
[[Category: Lowe J]]
[[Category: Archaea]]
[[Category: Cell shape]]
[[Category: Cytoskeleton]]
[[Category: Structural protein]]
[[Category: Tubulin]]

Latest revision as of 10:17, 1 May 2024

CetZ2 from Haloferax volcanii - GTPgS bound protofilamentCetZ2 from Haloferax volcanii - GTPgS bound protofilament

Structural highlights

4b45 is a 2 chain structure with sequence from Haloferax volcanii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CETZ2_HALVD Involved in cell shape control.[HAMAP-Rule:MF_01946][1]

See Also

References

  1. Duggin IG, Aylett CH, Walsh JC, Michie KA, Wang Q, Turnbull L, Dawson EM, Harry EJ, Whitchurch CB, Amos LA, Lowe J. CetZ tubulin-like proteins control archaeal cell shape. Nature. 2014 Dec 22. doi: 10.1038/nature13983. PMID:25533961 doi:http://dx.doi.org/10.1038/nature13983

4b45, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA