Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 Å resolution

Murayama, K.; Kato-Murayama, M.; Katsura, K.; Uchikubo-Kamo, T.; Yamaguchi-Hirafuji, M.; Kawazoe, M.; Akasaka, R.; Hanawa-Suetsugu, K.; Hori-Takemoto, C.; Terada, T.; Shirouzu, M.; Yokoyama, S.

doi:10.1107/S1744309104032555

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
Sequence alignment among structural homologues of APE2540. Blue bars and red arrows above the sequences show secondary-structural elements (α-helix and β-sheet). Identical amino acids are highlighted in red. The Lys residues conserved for deacylation activity are highlighted in green.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 61| Part 1| December 2005| Pages 26-29

doi:10.1107/S1744309104032555

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