1elp
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GAMMA-D CRYSTALLIN STRUCTURE AT 1.95 A RESOLUTION
OverviewOverview
The crystal structure of bovine lens gammaIIIb-crystallin at 2.5 A, resolution previously reported was interpreted using a consensus sequence, derived from related vertebrate sequences on the assumption that, gammaIIIb-crystallin derived from the gammaC-crystallin gene. It has, recently been shown that gammaIIIb is a product of the bovine gammaD gene., The structure of gammaIIIb has now been refined with the bovine gammaD, sequence using new 1.95 A resolution synchrotron data. The, crystallographic R factor was 20.4% for all 33 104 reflection data between, 8.0 and 1.95 A measured at 277(1) K. The electron density fully supported, the assignment of the gammaD sequence to gammaIIIb. The crystal belongs to, space group P2(1)2(1)2(1) with two molecules of molecular mass 20 749 Da, in the asymmetric unit in which 219 water molecules were located. The, two-domain four-Greek-key motif highly symmetrical protein is very similar, in structure to gammaB-crystallin (81% sequence identity). There is a, single amino-acid deletion in gammaD in the linker region connecting the, two domains. The intermolecular oganization in the crystal lattice is, quite different from gammaB as a result of key mutations involving surface, residues Leu51, Ile103 and His155. These point mutations will contribute, to the intermolecular behaviour of the gamma-crystallins in the eye lens, where they are major components of the densely packed, high refractive, index regions of the lens.
About this StructureAbout this Structure
1ELP is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of bovine eye lens gammaD (gammaIIIb)-crystallin at 1.95 A., Chirgadze YN, Driessen HP, Wright G, Slingsby C, Hay RE, Lindley PF, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):712-21. PMID:15299634
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