2bt8: Difference between revisions

Revision as of 17:41, 21 February 2008

STRUCTURE OF THE C-TERMINAL RECEPTOR-BINDING DOMAIN OF AVIAN REOVIRUS FIBRE SIGMAC, SPACE GROUP P6322.

OverviewOverview

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 StructureAbout this Structure

2BT8 is a Single protein structure of sequence from Avian orthoreovirus. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Avian orthoreovirus]]
 [[Category: Single protein]]
-[[Category: Calvo, P.Guardado.]]
+[[Category: Calvo, P Guardado.]]
-[[Category: Fox, G.C.]]
+[[Category: Fox, G C.]]
-[[Category: Llamas-Saiz, A.L.]]
+[[Category: Llamas-Saiz, A L.]]
-[[Category: Parrado, X.L.Hermo.]]
+[[Category: Parrado, X L.Hermo.]]
-[[Category: Raaij, M.J.Van.]]
+[[Category: Raaij, M J.Van.]]
 [[Category: beta-barrel]]
 [[Category: orthoreovirus]]
@@ Line 23: / Line 23: @@
 [[Category: viral protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:30:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:24 2008''