1f46: Difference between revisions

Revision as of 13:34, 21 February 2008

THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY

OverviewOverview

In Escherichia coli, FtsZ, a homologue of eukaryotic tubulins, and ZipA, a membrane-anchored protein that binds to FtsZ, are two essential components of the septal ring structure that mediates cell division. Recent data indicate that ZipA is involved in the assembly of the ring by linking FtsZ to the cytoplasmic membrane and that the ZipA-FtsZ interaction is mediated by their C-terminal domains. We present the X-ray crystal structures of the C-terminal FtsZ-binding domain of ZipA and a complex between this domain and a C-terminal fragment of FtsZ. The ZipA domain is a six-stranded beta-sheet packed against three alpha-helices and contains the split beta-alpha-beta motif found in many RNA-binding proteins. The uncovered side of the sheet incorporates a shallow hydrophobic cavity exposed to solvent. In the complex, the 17-residue FtsZ fragment occupies this entire cavity of ZipA and binds as an extended beta-strand followed by alpha-helix. An alanine-scanning mutagenesis analysis of the FtsZ fragment was also performed, which shows that only a small cluster of the buried FtsZ side chains is critical in binding to ZipA.

About this StructureAbout this Structure

1F46 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography., Mosyak L, Zhang Y, Glasfeld E, Haney S, Stahl M, Seehra J, Somers WS, EMBO J. 2000 Jul 3;19(13):3179-91. PMID:10880432

Page seeded by OCA on Thu Feb 21 12:34:38 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1f46.jpg|left|200px]]<br /><applet load="1f46" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1f46.jpg|left|200px]]<br /><applet load="1f46" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1f46, resolution 1.5&Aring;" />
 '''THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY'''<br />
 ==Overview==
-In Escherichia coli, FtsZ, a homologue of eukaryotic tubulins, and ZipA, a, membrane-anchored protein that binds to FtsZ, are two essential components, of the septal ring structure that mediates cell division. Recent data, indicate that ZipA is involved in the assembly of the ring by linking FtsZ, to the cytoplasmic membrane and that the ZipA-FtsZ interaction is mediated, by their C-terminal domains. We present the X-ray crystal structures of, the C-terminal FtsZ-binding domain of ZipA and a complex between this, domain and a C-terminal fragment of FtsZ. The ZipA domain is a, six-stranded beta-sheet packed against three alpha-helices and contains, the split beta-alpha-beta motif found in many RNA-binding proteins. The, uncovered side of the sheet incorporates a shallow hydrophobic cavity, exposed to solvent. In the complex, the 17-residue FtsZ fragment occupies, this entire cavity of ZipA and binds as an extended beta-strand followed, by alpha-helix. An alanine-scanning mutagenesis analysis of the FtsZ, fragment was also performed, which shows that only a small cluster of the, buried FtsZ side chains is critical in binding to ZipA.
+In Escherichia coli, FtsZ, a homologue of eukaryotic tubulins, and ZipA, a membrane-anchored protein that binds to FtsZ, are two essential components of the septal ring structure that mediates cell division. Recent data indicate that ZipA is involved in the assembly of the ring by linking FtsZ to the cytoplasmic membrane and that the ZipA-FtsZ interaction is mediated by their C-terminal domains. We present the X-ray crystal structures of the C-terminal FtsZ-binding domain of ZipA and a complex between this domain and a C-terminal fragment of FtsZ. The ZipA domain is a six-stranded beta-sheet packed against three alpha-helices and contains the split beta-alpha-beta motif found in many RNA-binding proteins. The uncovered side of the sheet incorporates a shallow hydrophobic cavity exposed to solvent. In the complex, the 17-residue FtsZ fragment occupies this entire cavity of ZipA and binds as an extended beta-strand followed by alpha-helix. An alanine-scanning mutagenesis analysis of the FtsZ fragment was also performed, which shows that only a small cluster of the buried FtsZ side chains is critical in binding to ZipA.
 ==About this Structure==
-F46 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F46 OCA].
+F46 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=1F46 OCA].
 ==Reference==
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 [[Category: Glasfeld, E.]]
 [[Category: Mosyak, L.]]
-[[Category: Somers, W.S.]]
+[[Category: Somers, W S.]]
 [[Category: Stahl, M.]]
 [[Category: Zhang, Y.]]
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 [[Category: transmembrane]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:35:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:38 2008''