1hdf
From Proteopedia
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EVOLUTION OF THE EYE LENS BETA-GAMMA-CRYSTALLIN DOMAIN FOLD
Overview
BACKGROUND: The betagamma-crystallins belong to a superfamily of, two-domain proteins found in vertebrate eye lenses, with distant relatives, occurring in microorganisms. It has been considered that an eukaryotic, stress protein, spherulin 3a, from the slime mold Physarum polycephalum, shares a common one-domain ancestor with crystallins, similar to the, one-domain 3-D structure determined by NMR. RESULTS: The X-ray structure, of spherulin 3a shows it to be a tight homodimer, which is consistent with, ultracentrifugation studies. The (two-motif) domain fold contains a pair, of calcium binding sites very similar to those found in a two-domain, prokaryotic betagamma-crystallin fold family member, Protein S. Domain, pairing in the spherulin 3a dimer is two-fold symmetric, but quite, ... [(full description)]
About this Structure
1HDF is a [Single protein] structure of sequence from [Physarum polycephalum] with CA as [ligand]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the calcium-loaded spherulin 3a dimer sheds light on the evolution of the eye lens betagamma-crystallin domain fold., Clout NJ, Kretschmar M, Jaenicke R, Slingsby C, Structure. 2001 Feb 7;9(2):115-24. PMID:11250196
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