1f46: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:


==THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY==
==THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY==
<StructureSection load='1f46' size='340' side='right' caption='[[1f46]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='1f46' size='340' side='right'caption='[[1f46]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1f46]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F46 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F46 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1f46]] is a 2 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=1F46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F46 FirstGlance]. <br>
</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=1f46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f46 OCA], [http://pdbe.org/1f46 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f46 RCSB], [http://www.ebi.ac.uk/pdbsum/1f46 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f46 ProSAT]</span></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]] 1.5&#8491;</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=1f46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f46 OCA], [https://pdbe.org/1f46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f46 RCSB], [https://www.ebi.ac.uk/pdbsum/1f46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f46 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ZIPA_ECOLI ZIPA_ECOLI]] Interacts directly with the cell division protein FtsZ. Probable receptor for the septal ring structure, may anchor it to the inner-membrane.[HAMAP-Rule:MF_00509]  
[https://www.uniprot.org/uniprot/ZIPA_ECOLI ZIPA_ECOLI] Interacts directly with the cell division protein FtsZ. Probable receptor for the septal ring structure, may anchor it to the inner-membrane.[HAMAP-Rule:MF_00509]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/1f46_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/1f46_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 18: Line 19:
</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=1f46 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=1f46 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In Escherichia coli, FtsZ, a homologue of eukaryotic tubulins, and ZipA, a membrane-anchored protein that binds to FtsZ, are two essential components of the septal ring structure that mediates cell division. Recent data indicate that ZipA is involved in the assembly of the ring by linking FtsZ to the cytoplasmic membrane and that the ZipA-FtsZ interaction is mediated by their C-terminal domains. We present the X-ray crystal structures of the C-terminal FtsZ-binding domain of ZipA and a complex between this domain and a C-terminal fragment of FtsZ. The ZipA domain is a six-stranded beta-sheet packed against three alpha-helices and contains the split beta-alpha-beta motif found in many RNA-binding proteins. The uncovered side of the sheet incorporates a shallow hydrophobic cavity exposed to solvent. In the complex, the 17-residue FtsZ fragment occupies this entire cavity of ZipA and binds as an extended beta-strand followed by alpha-helix. An alanine-scanning mutagenesis analysis of the FtsZ fragment was also performed, which shows that only a small cluster of the buried FtsZ side chains is critical in binding to ZipA.


The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography.,Mosyak L, Zhang Y, Glasfeld E, Haney S, Stahl M, Seehra J, Somers WS EMBO J. 2000 Jul 3;19(13):3179-91. PMID:10880432<ref>PMID:10880432</ref>
==See Also==
 
*[[Cell division protein 3D structures|Cell division protein 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1f46" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glasfeld, E]]
[[Category: Escherichia coli]]
[[Category: Mosyak, L]]
[[Category: Large Structures]]
[[Category: Somers, W S]]
[[Category: Glasfeld E]]
[[Category: Stahl, M]]
[[Category: Mosyak L]]
[[Category: Zhang, Y]]
[[Category: Somers WS]]
[[Category: Cell cycle]]
[[Category: Stahl M]]
[[Category: Cell division]]
[[Category: Zhang Y]]
[[Category: Cell division protein zipa]]
[[Category: Inner membrane]]
[[Category: Transmembrane]]

Latest revision as of 10:10, 7 February 2024

THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHYTHE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY

Structural highlights

1f46 is a 2 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 1.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ZIPA_ECOLI Interacts directly with the cell division protein FtsZ. Probable receptor for the septal ring structure, may anchor it to the inner-membrane.[HAMAP-Rule:MF_00509]

Evolutionary Conservation

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

See Also

1f46, resolution 1.50Å

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
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1f46&oldid=4043162"