Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster.
The crystal structure of the dimerization domain of the V(D)J recombination-activating protein, RAG1, was solved using zinc anomalous scattering. The structure reveals an unusual combination of multi-class zinc-binding motifs, including a zinc RING finger and a C2H2 zinc finger, that together from a single structural domain. The domain also contains a unique zinc binuclear cluster in place of a normally mononuclear zinc site in the RING finger. Together, four zinc ions help organize the entire domain, including the two helices that form the dimer interface.
Bellon
S F
SF
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA.
Rodgers
K K
KK
Schatz
D G
DG
Coleman
J E
JE
Steitz
T A
TA
D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D019281:Dimerization; D018398:Homeodomain Proteins; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011487:Protein Conformation; D015032:Zinc / Q000378:metabolism*; D016335:Zinc Fingers
D004268:DNA-Binding Proteins; D018398:Homeodomain Proteins; C064658:RAG-1 protein; D015032:Zinc