1opo

From Proteopedia

---

Revision as of 20:58, 20 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1opo, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE STRUCTURE OF CARNATION MOTTLE VIRUS

Overview

The structure of the Carnation Mottle Virus (CMtV) capsid protein has been, determined at 3.2 A resolution by the method of molecular replacement., Three-dimensional data were collected from a small number of crystals, (sp.g. I23, a = 382.6 A) using the synchrotron radiation with an image, plate as detector. The coordinates of Tomato Bushy Stunt Virus (TBSV) were, used as a searching model. Refinement of the coordinates of 7,479, non-hydrogen atoms performed by the program XPLOR, has led to an R-factor, of 18.3%. It was found that the amino acid chain fold of capsid protein is, very similar to that in other icosahedral viruses. However, there are some, differences in the contact regions between protein subunits and also the, lack of the beta-annulus around the 3-fold icosahedral axes. The, structural and biochemical results lead us to consider an alternative, assembly pathway.

About this Structure

1OPO is a Single protein structure of sequence from Carnation mottle virus with SO4 and CA as ligands. Full crystallographic information is available from OCA.

Reference

The atomic structure of Carnation Mottle Virus capsid protein., Morgunova EYu, Dauter Z, Fry E, Stuart DI, Stel'mashchuk VYa, Mikhailov AM, Wilson KS, Vainshtein BK, FEBS Lett. 1994 Feb 7;338(3):267-71. PMID:8307192

Page seeded by OCA on Tue Nov 20 23:05:27 2007