The X-ray crystal structure of human gamma S-crystallin C-terminal domain.
gammaS-crystallin is a major human lens protein found in the outer region of the eye lens, where the refractive index is low. Because crystallins are not renewed they acquire post-translational modifications that may perturb stability and solubility. In common with other members of the betagamma-crystallin superfamily, gammaS-crystallin comprises two similar beta-sheet domains. The crystal structure of the C-terminal domain of human gammaS-crystallin has been solved at 2.4 A resolution. The structure shows that in the in vitro expressed protein, the buried cysteines remain reduced. The backbone conformation of the "tyrosine corner" differs from that of other betagamma-crystallins because of deviation from the consensus sequence. The two C-terminal domains in the asymmetric unit are organized about a slightly distorted 2-fold axis to form a dimer with similar geometry to full-length two-domain family members. Two glutamines found in lattice contacts may be important for short range interactions in the lens. An asparagine known to be deamidated in human cataract is located in a highly ordered structural region.
Purkiss
Andrew G
AG
School of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, United Kingdom . a.purkiss@mail.cryst.bbk.ac.uk
Bateman
Orval A
OA
Goodfellow
Julia M
JM
Lubsen
Nicolette H
NH
Slingsby
Christine
C
D000818:Animals; D001483:Base Sequence; D003459:Crystallins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000378:metabolism; D017931:DNA Primers; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D014443:Tyrosine / Q000378:metabolism
D003459:Crystallins; D017931:DNA Primers; D014443:Tyrosine; D003545:Cysteine