1f7w: Difference between revisions

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 ==SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA==
-<StructureSection load='1f7w' size='340' side='right'caption='[[1f7w]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1f7w' size='340' side='right'caption='[[1f7w]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1f7w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F7W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1f7w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F7W FirstGlance]. <br>
-</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=1f7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7w OCA], [https://pdbe.org/1f7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f7w RCSB], [https://www.ebi.ac.uk/pdbsum/1f7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7w ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1f7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7w OCA], [https://pdbe.org/1f7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f7w RCSB], [https://www.ebi.ac.uk/pdbsum/1f7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7w 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]
+[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]]
@@ 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=1f7w ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-ZipA, an essential component of cell division in Escherichia coli, interacts with the FtsZ protein at the midcell in one of the initial steps of septum formation. The high-resolution solution structure of the 144-residue C-terminal domain of E. coli ZipA (ZipA(185)(-)(328)) has been determined by multidimensional heteronuclear NMR. A total of 30 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of 2758 experimental NMR restraints. The atomic root means square distribution about the mean coordinate positions for residues 6-142 for the 30 structures is 0.37 +/- 0.04 A for the backbone atoms, 0. 78 +/- 0.05 A for all atoms, and 0.45 +/- 0.04 A for all atoms excluding disordered side chains. The NMR solution structure of ZipA(185)(-)(328) is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands where the alpha-helices and the beta-sheet form surfaces directly opposite each other. A C-terminal peptide from FtsZ has been shown to bind ZipA(185)(-)(328) in a hydrophobic channel formed by the beta-sheet providing insight into the ZipA-FtsZ interaction. An unexpected similarity between the ZipA(185)(-)(328) fold and the split beta-alpha-beta fold observed in many RNA binding proteins may further our understanding of the critical ZipA-FtsZ interaction.
-Solution structure of ZipA, a crucial component of Escherichia coli cell division.,Moy FJ, Glasfeld E, Mosyak L, Powers R Biochemistry. 2000 Aug 8;39(31):9146-56. PMID:10924108<ref>PMID:10924108</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1f7w" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Cell division protein 3D structures|Cell division protein 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Glasfeld, E]]
+[[Category: Glasfeld E]]
-[[Category: Mosyak, L]]
+[[Category: Mosyak L]]
-[[Category: Moy, F J]]
+[[Category: Moy FJ]]
-[[Category: Powers, R]]
+[[Category: Powers R]]
-[[Category: Alpha-beta fold]]
-[[Category: Cell cycle]]
-[[Category: Cell division]]
-[[Category: Septation]]
-[[Category: Transmembrane]]