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1f47

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

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Retrieved from "http://52.214.119.220/wiki/index.php/1f47"

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-[[Image:1f47.jpg|left|200px]]<br /><applet load="1f47" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1f47, resolution 1.95&Aring;" />
-'''THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY'''<br />
-==Overview==
+==THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY==
-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.
+<StructureSection load='1f47' size='340' side='right'caption='[[1f47]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1f47]] 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=1F47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F47 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#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=1f47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f47 OCA], [https://pdbe.org/1f47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f47 RCSB], [https://www.ebi.ac.uk/pdbsum/1f47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f47 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/1f47_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/main_output.php?pdb_ID=1f47 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-F47 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F47 OCA].
+*[[Cell division protein 3D structures|Cell division protein 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10880432 10880432]
 [[Category: Escherichia coli]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Glasfeld, E.]]
+[[Category: Glasfeld E]]
-[[Category: Mosyak, L.]]
+[[Category: Mosyak L]]
-[[Category: Somers, W.S.]]
+[[Category: Somers WS]]
-[[Category: Stahl, M.]]
+[[Category: Stahl M]]
-[[Category: Zhang, Y.]]
+[[Category: Zhang Y]]
-[[Category: cell division ftsz]]
-[[Category: cell division zipa]]
-[[Category: inner membrane]]
-[[Category: separation]]
-[[Category: transmembrane]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:35:39 2007''

1f47

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

Structural highlights

Function

Evolutionary Conservation

See Also

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