1f7x: Difference between revisions
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<StructureSection load='1f7x' size='340' side='right' caption='[[1f7x]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | <StructureSection load='1f7x' size='340' side='right' caption='[[1f7x]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://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=1F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7X FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f7w|1f7w]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f7w|1f7w]]</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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x PDBsum]</span></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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://pdbe.org/1f7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1f7x" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Glasfeld, E]] | [[Category: Glasfeld, E]] | ||
[[Category: Mosyak, L]] | [[Category: Mosyak, L]] | ||
Revision as of 13:03, 10 September 2015
SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPASOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA
Structural highlights
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. Publication Abstract from PubMedZipA, 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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