This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4uy3

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Cytoplasmic domain of bacterial cell division protein ezra

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4uy3"

@@ Line 1: / Line 1: @@
 ==Cytoplasmic domain of bacterial cell division protein ezra==
-<StructureSection load='4uy3' size='340' side='right' caption='[[4uy3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='4uy3' size='340' side='right'caption='[[4uy3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4uy3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UY3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4uy3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UY3 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uxv|4uxv]]</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]] 2.6&#8491;</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=4uy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uy3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uy3 RCSB], [http://www.ebi.ac.uk/pdbsum/4uy3 PDBsum]</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=4uy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uy3 OCA], [https://pdbe.org/4uy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uy3 RCSB], [https://www.ebi.ac.uk/pdbsum/4uy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uy3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/EZRA_STAA1 EZRA_STAA1]] Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.
+[https://www.uniprot.org/uniprot/EZRA_STAA1 EZRA_STAA1] Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Bacterial cell division is facilitated by a molecular machine-the divisome-that assembles at mid-cell in dividing cells. The formation of the cytokinetic Z-ring by the tubulin homologue FtsZ is regulated by several factors, including the divisome component EzrA. Here we describe the structure of the 60-kDa cytoplasmic domain of EzrA, which comprises five linear repeats of an unusual triple helical bundle. The EzrA structure is bent into a semicircle, providing the protein with the potential to interact at both N- and C-termini with adjacent membrane-bound divisome components. We also identify at least two binding sites for FtsZ on EzrA and map regions of EzrA that are responsible for regulating FtsZ assembly. The individual repeats, and their linear organization, are homologous to the spectrin proteins that connect actin filaments to the membrane in eukaryotes, and we thus propose that EzrA is the founding member of the bacterial spectrin family.
-Structure and function of a spectrin-like regulator of bacterial cytokinesis.,Cleverley RM, Barrett JR, Basle A, Bui NK, Hewitt L, Solovyova A, Xu ZQ, Daniel RA, Dixon NE, Harry EJ, Oakley AJ, Vollmer W, Lewis RJ Nat Commun. 2014 Nov 18;5:5421. doi: 10.1038/ncomms6421. PMID:25403286<ref>PMID:25403286</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Barrett, J R]]
+[[Category: Large Structures]]
-[[Category: Basle, A]]
+[[Category: Staphylococcus aureus]]
-[[Category: Cleverley, R M]]
+[[Category: Barrett JR]]
-[[Category: Daniela, R A]]
+[[Category: Basle A]]
-[[Category: Dixon, N E]]
+[[Category: Cleverley RM]]
-[[Category: Harry, E J]]
+[[Category: Daniela RA]]
-[[Category: Hewitt, L]]
+[[Category: Dixon NE]]
-[[Category: Khai-Bui, N]]
+[[Category: Harry EJ]]
-[[Category: Lewis, R J]]
+[[Category: Hewitt L]]
-[[Category: Oakley, A J]]
+[[Category: Khai-Bui N]]
-[[Category: Solovyova, A]]
+[[Category: Lewis RJ]]
-[[Category: Vollmer, W]]
+[[Category: Oakley AJ]]
-[[Category: Xu, Z]]
+[[Category: Solovyova A]]
-[[Category: Cell wall]]
+[[Category: Vollmer W]]
-[[Category: Divisome]]
+[[Category: Xu Z]]
-[[Category: Ftsz]]
-[[Category: Spectrin]]
-[[Category: Structural protein]]
-[[Category: Tubulin]]
-[[Category: Z-ring]]

4uy3

From Proteopedia

Current revision

Cytoplasmic domain of bacterial cell division protein ezra

Structural highlights

Function

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox