1f47: Difference between revisions
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'''THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY''' | {{Structure | ||
|PDB= 1f47 |SIZE=350|CAPTION= <scene name='initialview01'>1f47</scene>, resolution 1.95Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F47 is a [ | 1F47 is a [[Protein complex]] structure of sequences 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=1F47 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10880432 10880432] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:11 2008'' | ||
Revision as of 12:04, 20 March 2008
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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
1F47 is a Protein complex structure of sequences 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
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