Quaternary structure of alpha-crustacyanin from lobster as seen by small-angle X-ray scattering.
The structure of alpha-crustacyanin, the blue carotenoprotein of lobster (Homarus gammarus) carapace, has been investigated for the first time using small-angle X-ray scattering. In this paper, we have determined the dimensions of this protein composed of eight heterodimeric subunits of beta-crustacyanin. Analysis of the scattering spectra and estimation of the shape of alpha-crustacyanin show that the protein fits into a cylinder with an axial length of 238 A and a radius of 47.5 A, in which the eight beta-crustacyanin molecules are probably arranged in a helical manner.
Dellisanti
Cosma D
CD
School of Biochemistry and Molecular Biology, University of Leeds, Mount Preston Street, UK.
Spinelli
Silvia
S
Cambillau
Christian
C
Findlay
John B C
JB
Zagalsky
Peter F
PF
Finet
Stéphanie
S
Receveur-Bréchot
Véronique
V
D000818:Animals; D002338:Carotenoids / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008121:Nephropidae; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012542:Scattering, Radiation; D014961:X-Ray Diffraction / Q000379:methods*; D014965:X-Rays
D002352:Carrier Proteins; D011506:Proteins; C018494:crustacyanins; D002338:Carotenoids