The C-terminal domains of gammaS-crystallin pair about a distorted twofold axis.
The 2-domain gammaS-crystallin, a highly conserved early evolutionary off-shoot of the gamma-crystallin family, is located in the water-rich region of eye lenses. The expressed C-terminal domain, gammaS-C, has been crystallized and the 2.56 A X-ray structure determined. There are two domains in the asymmetric unit which pair about a distorted twofold axis. One of the domains has an altered conformation in a highly conserved region of the protein, the tyrosine corner. The distorted gammaS-C dimer of domains is compared with the highly symmetrical, equivalent recombinant dimer of C-terminal domains from gammaB-crystallin. Sequence changes close to the interface, that distinguish gammaS from the other gamma-crystallins, are examined in order to evaluate their role in symmetrical domain pairing.
Basak
A K
AK
Department of Crystallography, Birkbeck College, London, UK.
Kroone
R C
RC
Lubsen
N H
NH
Naylor
C E
CE
Jaenicke
R
R
Slingsby
C
C
D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics; D008958:Models, Molecular; D016296:Mutagenesis; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D014443:Tyrosine
D003459:Crystallins; D011994:Recombinant Proteins; D014443:Tyrosine