1xi7
From Proteopedia
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'''NMR structure of the carboxyl-terminal cysteine domain of the VHv1.1 polydnaviral gene product''' | '''NMR structure of the carboxyl-terminal cysteine domain of the VHv1.1 polydnaviral gene product''' | ||
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[[Category: Jaseja, M.]] | [[Category: Jaseja, M.]] | ||
[[Category: Webb, B.]] | [[Category: Webb, B.]] | ||
| - | [[Category: | + | [[Category: Antiparallel beta sheet structural scaffold]] |
| - | [[Category: | + | [[Category: Cystine knot]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:03:53 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:03, 3 May 2008
NMR structure of the carboxyl-terminal cysteine domain of the VHv1.1 polydnaviral gene product
Overview
Polydnaviruses are an unusual group of insect viruses that have an obligate symbiotic association with certain parasitic wasps. These viruses are transmitted with the wasp egg during oviposition into lepidopteran insects, enabling the survival and development of the egg inside the host larvae. We report the three-dimensional structure of a novel polydnaviral cysteine-rich motif (cys-motif), identified as the carboxyl-terminal domain of a two cys-motif containing polydnaviral VHv1.1 gene product, abbreviated "C-term VHv1.1". This 65-residue domain was identified experimentally by limited proteolysis of the full-length protein and was subsequently cloned in a bacterial expression system for NMR studies. The C-term VHv1.1 3D structure was determined in solution by two-dimensional (1)H NMR spectroscopy. Calculation of the structure was based on a total of 300 upper distance restraints and 20 dihedral angle constraints, and resulted in an ensemble of 25 representative conformers with an average rmsd of 0.47 A from the mean structure for core backbone atoms. The protein core is made of a four beta-strand scaffold held together in a compact structure by three disulfide bonds, which form a cystine knot. The four beta-strands are arranged in an unusual configuration to form a triple-stranded beta-sheet and double-stranded beta-sheet. Comparison with other classes of cystine knots provides indication that C-term VHv1.1 represents a new and distinct cystine knot motif. This analysis provides a structural basis for interpretation of the genetic and amino acid sequence data classifying polydnavirus gene products as members of cysteine-rich protein families.
About this Structure
1XI7 is a Single protein structure of sequence from Campoletis sonorensis ichnovirus. Full crystallographic information is available from OCA.
Reference
Solution structure of the carboxyl-terminal cysteine-rich domain of the VHv1.1 polydnaviral gene product: comparison with other cystine knot structural folds., Einerwold J, Jaseja M, Hapner K, Webb B, Copie V, Biochemistry. 2001 Dec 4;40(48):14404-12. PMID:11724552 Page seeded by OCA on Sat May 3 15:03:53 2008
