1f7x
From Proteopedia
(New page: 200px<br /><applet load="1f7x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f7x" /> '''SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA...) |
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| - | [[Image:1f7x.gif|left|200px]]<br /><applet load="1f7x" size=" | + | [[Image:1f7x.gif|left|200px]]<br /><applet load="1f7x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f7x" /> | caption="1f7x" /> | ||
'''SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA'''<br /> | '''SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA'''<br /> | ||
==Overview== | ==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 | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1F7X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1F7X is a [http://en.wikipedia.org/wiki/Single_protein 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]. |
==Reference== | ==Reference== | ||
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[[Category: Glasfeld, E.]] | [[Category: Glasfeld, E.]] | ||
[[Category: Mosyak, L.]] | [[Category: Mosyak, L.]] | ||
| - | [[Category: Moy, F | + | [[Category: Moy, F J.]] |
[[Category: Powers, R.]] | [[Category: Powers, R.]] | ||
[[Category: alpha-beta fold]] | [[Category: alpha-beta fold]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:56 2008'' |
Revision as of 10:35, 21 February 2008
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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.
About this Structure
1F7X is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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