1amm
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1amm.jpg|left|200px]]<br /><applet load="1amm" size=" | + | [[Image:1amm.jpg|left|200px]]<br /><applet load="1amm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1amm, resolution 1.2Å" /> | caption="1amm, resolution 1.2Å" /> | ||
'''1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K'''<br /> | '''1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K'''<br /> | ||
==Overview== | ==Overview== | ||
| - | gammabeta-crystallin is a structural protein of the eye lens with a role | + | 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== | ==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:// | + | 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]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Glover, I | + | [[Category: Glover, I D.]] |
| - | [[Category: Kumaraswamy, V | + | [[Category: Kumaraswamy, V S.]] |
| - | [[Category: Lindley, P | + | [[Category: Lindley, P F.]] |
[[Category: Slingsby, C.]] | [[Category: Slingsby, C.]] | ||
[[Category: crystallin]] | [[Category: crystallin]] | ||
[[Category: eye lens protein]] | [[Category: eye lens protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:06 2008'' |
Revision as of 09:46, 21 February 2008
|
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 Feb 21 11:46:06 2008
