2bsf: Difference between revisions

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[[Image:2bsf.gif|left|200px]]
{{Seed}}
[[Image:2bsf.png|left|200px]]


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{{STRUCTURE_2bsf|  PDB=2bsf  |  SCENE=  }}  
{{STRUCTURE_2bsf|  PDB=2bsf  |  SCENE=  }}  


'''STRUCTURE OF THE C-TERMINAL RECEPTOR-BINDING DOMAIN OF AVIAN REOVIRUS FIBRE SIGMAC, ZN CRYSTAL FORM.'''
===STRUCTURE OF THE C-TERMINAL RECEPTOR-BINDING DOMAIN OF AVIAN REOVIRUS FIBRE SIGMAC, ZN CRYSTAL FORM.===




==Overview==
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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.
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{{ABSTRACT_PUBMED_16236316}}


==About this Structure==
==About this Structure==
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[[Category: Triple beta-spiral]]
[[Category: Triple beta-spiral]]
[[Category: Viral protein]]
[[Category: Viral protein]]
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