From Proteopedia
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| | {{STRUCTURE_1amm| PDB=1amm | SCENE= }} | | {{STRUCTURE_1amm| PDB=1amm | SCENE= }} |
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| - | '''1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K'''
| + | ===1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15299624}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15299624 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15299624}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Crystallin]] | | [[Category: Crystallin]] |
| | [[Category: Eye lens protein]] | | [[Category: Eye lens protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:27:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:10:07 2008'' |
Revision as of 14:10, 30 June 2008
Template:STRUCTURE 1amm
1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K
Template:ABSTRACT PUBMED 15299624
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
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