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.
1amm
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1amm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1amm, resolution 1.2Å" /> '''1.2 ANGSTROM STRUCTUR...)
Next diff →
Revision as of 08:50, 20 November 2007
|
1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K
Overview
gammabeta-crystallin is a structural protein of the eye lens with a role, in the maintenance of an even distribution of protein and water over, distances around the wavelength of light, preserving lens transparency., The structure of the 174-residue bovine protein has already been, determined at room temperature to 1.47 A resolution. By flash freezing the, protein crystals, data have now been collected to a nominal resolution, limit of 1.2 A as radiation damage was essentially eliminated. The, protein-water model has been refined against this data using the program, RESTRAIN converging to an R factor of 18.5% with all data. Atomic, positions are clearly indicated in the electron-density maps. Discrete, bimodal disorder has been visualized for a few side chains. Out of a total, of 498 water molecules present in the crystal asymmetric unit, 394 have, been modelled and refined at unit occupancy. The solvent structure is, extremely well ordered with an average B value of 23.4 A(2). Partially, occupied sites have been identified where disorder in the protein induces, concomitant disorder in the local solvent structure. The solvent structure, covers 97% of the solvent-exposed surface of the protein in the crystal., 126 water molecules are distributed in second and higher hydration shells., There are networks of hydrogen-bonded solvent extending up to 64 molecules, in a network, comprising trimers and tetramers as well as five- and, six-membered water-ring structures. The hydration of the protein surface, is dominated by arginine and aspartate side chains. Extensive cages of, highly ordered solvent molecules are also observed around exposed, non-polar groups.
About this Structure
1AMM is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
An eye lens protein-water structure: 1.2 A resolution structure of gammaB-crystallin at 150 K., Kumaraswamy VS, Lindley PF, Slingsby C, Glover ID, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):611-22. PMID:15299624
Page seeded by OCA on Tue Nov 20 10:57:51 2007
