This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1phs

From Proteopedia

Revision as of 12:29, 21 February 2008 by OCA (Talk | contribs)
Jump to: navigation, search
Image:1phs.gif

1phs, resolution 3.0Å

Drag the structure with the mouse to rotate

THE THREE-DIMENSIONAL STRUCTURE OF THE SEED STORAGE PROTEIN PHASEOLIN AT 3 ANGSTROMS RESOLUTION

Overview

The polypeptides of the trimeric seed storage protein phaseolin comprise two structurally similar units each made up of a beta-barrel and an alpha-helical domain. The beta-barrel has the 'jelly-roll' folding topology of the viral coat proteins and the alpha-helical domain shows structural similarity to the helix-turn-helix motif found in certain DNA-binding proteins.

About this Structure

1PHS is a Single protein structure of sequence from Phaseolus vulgaris. Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution., Lawrence MC, Suzuki E, Varghese JN, Davis PC, Van Donkelaar A, Tulloch PA, Colman PM, EMBO J. 1990 Jan;9(1):9-15. PMID:2295315

Page seeded by OCA on Thu Feb 21 14:29:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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