1ohf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ohf.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ohf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ohf| PDB=1ohf | SCENE= }}
{{STRUCTURE_1ohf| PDB=1ohf | SCENE= }}
-
'''THE REFINED STRUCTURE OF NUDAURELIA CAPENSIS OMEGA VIRUS'''
+
===THE REFINED STRUCTURE OF NUDAURELIA CAPENSIS OMEGA VIRUS===
-
==Overview==
+
<!--
-
Large-scale reorganization of protein interactions characterizes many biological processes, yet few systems are accessible to biophysical studies that display this property. The capsid protein of Nudaurelia capensis omega Virus (NomegaV) has previously been characterized in two dramatically different T = 4 quasi-equivalent assembly states when expressed as virus-like particles (VLPs) in a baculovirus system. The procapsid (pH 7), is round, porous, and approximately 450 A in diameter. It converts, in vitro, to the capsid form at pH 5 and the capsid is sealed shut, shaped like an icosahedron, has a maximum diameter of 410 A and undergoes an autocatalytic cleavage at residue 570. Residues 571-644, the gamma peptide, remain associated with the particle and are partially ordered. The interconversion of these states has been previously studied by solution X-ray scattering, electron cryo microscopy (CryoEM), and site-directed mutagenesis. The particle structures appear equivalent in authentic virions and the low pH form of the expressed and assembled protein. Previously, and before the discovery of the multiple morphological forms of the VLPs, we reported the X-ray structure of authentic NomegaV at 2.8 A resolution. These coordinates defined the fold of the protein but were not refined at the time because of technical issues associated with the approximately 2.5 million reflection data set. We now report the refined, authentic virus structure that has added 29 residues to the original model and allows the description of the chemistry of molecular switching for T = 4 capsid formation and the multiple morphological forms. The amino and carboxy termini are internal, predominantly helical, and disordered to different degrees in the four structurally independent subunits; however, the refined structure shows significantly more ordered residues in this region, particularly at the amino end of the B subunit that is now seen to invade space occupied by the A subunits. These additional residues revealed a previously unnoticed strong interaction between the pentameric, gamma peptide helices of the A and B subunits that are largely proximal to the quasi-6-fold axes. One C-terminal helix is ordered in the C and D subunits and stabilizes a flat interaction in two interfaces between the protein monomers while the other, quasi-equivalent, interactions are bent. As this helix is arginine rich, the comparable, disordered region in the A and B subunits probably interacts with RNA. One of the subunit-subunit interfaces has an unusual arrangement of carboxylate side chains. Based on this observation, we propose a mechanism for the control of the pH-dependent transitions of the virus particle.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14972547}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14972547 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14972547}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Quasiequivalence]]
[[Category: Quasiequivalence]]
[[Category: Viral coat]]
[[Category: Viral coat]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:51:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:34:34 2008''

Revision as of 09:34, 28 July 2008

Image:1ohf.png

Template:STRUCTURE 1ohf

THE REFINED STRUCTURE OF NUDAURELIA CAPENSIS OMEGA VIRUS

Template:ABSTRACT PUBMED 14972547

About this Structure

1OHF is a Single protein structure of sequence from Nudaurelia capensis omega virus. Full crystallographic information is available from OCA.

Reference

The refined structure of Nudaurelia capensis omega virus reveals control elements for a T = 4 capsid maturation., Helgstrand C, Munshi S, Johnson JE, Liljas L, Virology. 2004 Jan 5;318(1):192-203. PMID:14972547

Page seeded by OCA on Mon Jul 28 12:34:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ohf"
Personal tools