2bsf
From Proteopedia
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|PDB= 2bsf |SIZE=350|CAPTION= <scene name='initialview01'>2bsf</scene>, resolution 2.10Å | |PDB= 2bsf |SIZE=350|CAPTION= <scene name='initialview01'>2bsf</scene>, resolution 2.10Å | ||
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsf OCA], [http://www.ebi.ac.uk/pdbsum/2bsf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bsf RCSB]</span> | ||
}} | }} | ||
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[[Category: Parrado, X L.Hermo.]] | [[Category: Parrado, X L.Hermo.]] | ||
[[Category: Raaij, M J.Van.]] | [[Category: Raaij, M J.Van.]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
[[Category: orthoreovirus]] | [[Category: orthoreovirus]] | ||
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[[Category: viral protein]] | [[Category: viral protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:11:05 2008'' |
Revision as of 23:11, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE C-TERMINAL RECEPTOR-BINDING DOMAIN OF AVIAN REOVIRUS FIBRE SIGMAC, ZN CRYSTAL FORM.
Overview
Avian reovirus fibre, a homo-trimer of the sigmaC protein, is responsible for primary host cell attachment. The protein expressed in bacteria forms elongated fibres comprised of a carboxy-terminal globular head domain and a slender shaft, and partial proteolysis yielded a carboxy-terminal protease-stable domain that was amenable to crystallisation. Here, we show that this fragment retains receptor-binding capability and report its structure, solved using two-wavelength anomalous diffraction and refined using data collected from three different crystal forms at 2.1 angstroms, 2.35 angstroms and 3.0 angstroms resolution. The carboxy-terminal globular domain has a beta-barrel fold with the same overall topology as the mammalian reovirus fibre (sigma1). However, the monomers of the sigmaC trimer show a more splayed-out arrangement than in the sigma1 structure. Also resolved are two triple beta-spiral repeats of the shaft or stalk domain. The presence in the sequence of heptad repeats amino-terminal to these triple beta-spiral repeats suggests that the unresolved portion of the shaft domain contains a triple alpha-helical coiled-coil structure. Implications for the function and stability of the sigmaC protein are discussed.
About this Structure
2BSF is a Single protein structure of sequence from Avian orthoreovirus. Full crystallographic information is available from OCA.
Reference
Structure of the carboxy-terminal receptor-binding domain of avian reovirus fibre sigmaC., Guardado Calvo P, Fox GC, Hermo Parrado XL, Llamas-Saiz AL, Costas C, Martinez-Costas J, Benavente J, van Raaij MJ, J Mol Biol. 2005 Nov 18;354(1):137-49. Epub 2005 Sep 30. PMID:16236316
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