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==SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA==
==SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA==
<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]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1f7x]] 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=1F7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F7X FirstGlance]. <br>
<table><tr><td colspan='2'>[[1f7x]] 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=1F7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F7X FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f7w|1f7w]]</div></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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [https://pdbe.org/1f7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [https://www.ebi.ac.uk/pdbsum/1f7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7x ProSAT]</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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [https://pdbe.org/1f7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [https://www.ebi.ac.uk/pdbsum/1f7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1f7x 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=1f7x ConSurf].
<div style="clear:both"></div>
<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 1f7x" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cell division protein 3D structures|Cell division protein 3D structures]]
*[[Cell division protein 3D structures|Cell division protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[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: Inner membrane]]
[[Category: Septation]]
[[Category: Transmembrane]]

Revision as of 13:11, 20 March 2024

SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPASOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA

Structural highlights

1f7x is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
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

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OCA
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