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Figure 1
The crystal structure of A. pernix fibrillarin bound to the SAM cofactor. The fibrillarin molecule is approximately 48 Å long and 32 Å wide. The N-terminal domain (residues 1–56) consists of five β-strands. The C-terminal domain (57–229) consists of seven β-strands that are sandwiched between seven α-helices. The SAM cofactor is positioned perpendicular to the β-sheet of the C-terminal domain.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 68| Part 8| July 2012| Pages 854-859
doi:10.1107/S1744309112026528
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