1HDF

Evolution of the eye lens beta-gamma-crystallin domain fold

Summary for 1HDF

Entry DOI	10.2210/pdb1hdf/pdb
Related	1AG4
Descriptor	SPHERULIN 3A, CALCIUM ION (3 entities in total)
Functional Keywords	structural protein, crystallins, eye lens, domain interactions, spherulin 3a, tyrosine corner
Biological source	PHYSARUM POLYCEPHALUM
Total number of polymer chains	2
Total formula weight	22620.99
Authors	Clout, N.J.,Kretschmar, M.,Jaenicke, R.,Slingsby, C. (deposition date: 2000-11-13, release date: 2000-12-28, Last modification date: 2024-11-06)
Primary citation	Clout, N.J.,Kretschmar, M.,Jaenicke, R.,Slingsby, C. Crystal Structure of the Calcium-Loaded Spherulin 3A Dimer Sheds Light on the Evolution of the Eye Lens Betagamma-Crystallin Domain Fold Structure, 9:115-, 2001 Cited by PubMed Abstract: 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. PubMed: 11250196 DOI: 10.1016/S0969-2126(01)00573-1 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.35 Å)

Structure validation