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

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1amm.jpg|left|200px]]<br /><applet load="1amm" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1amm.jpg|left|200px]]
-
caption="1amm, resolution 1.2&Aring;" />
+
 
-
'''1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K'''<br />
+
{{Structure
 +
|PDB= 1amm |SIZE=350|CAPTION= <scene name='initialview01'>1amm</scene>, resolution 1.2&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1AMM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMM OCA].
+
1AMM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMM OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299624 15299624]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/15299624 15299624]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 20: Line 29:
[[Category: eye lens protein]]
[[Category: eye lens protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:06 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:35 2008''

Revision as of 07:59, 20 March 2008


PDB ID 1amm

Drag the structure with the mouse to rotate
, resolution 1.2Å
Coordinates: save as pdb, mmCIF, xml



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 Thu Mar 20 09:59:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools