1f7x: Difference between revisions

Revision as of 02:50, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1f7x.png

Template:STRUCTURE 1f7x

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

Template:ABSTRACT PUBMED 10924108

About this StructureAbout this Structure

1F7X is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 1 02:50:33 2008

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OCA

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-[[Image:1f7x.gif|left|200px]]
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-'''SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA'''
+===SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10924108}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10924108 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10924108}}
 ==About this Structure==
-F7X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA].
+F7X is a [[Single protein]] structure of sequence from [http://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].
 ==Reference==
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 [[Category: Septation]]
 [[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:00:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:50:33 2008''