Structure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann-like folds that combine to form a unique active site with a possible role in heavy-metal chelation

Miller, M.D.; Aravind, L.; Bakolitsa, C.; Rife, C.L.; Carlton, D.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Chiu, H.-J.; Clayton, T.; Deller, M.C.; Duan, L.; Feuerhelm, J.; Grant, J.C.; Han, G.W.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Kozbial, P.; Krishna, S.S.; Kumar, A.; Marciano, D.; McMullan, D.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Reyes, R.; van den Bedem, H.; Weekes, D.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Elsliger, M.-A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.

doi:10.1107/S1744309110007517

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
Stereo ribbon diagram showing the structural superposition of (a) the C-terminal domain of Dhaf4260 (PDB code 3l5o ; residues 110–251; salmon) and precorrin-8w methyltransferase from Methanobacterium thermoautotrophicum (MT0146; PDB code 1f38 ; residues 1–186; gold) and (b) the N-terminal domain of Dhaf4260 (PDB code 3l5o ; residues 1–102; blue) and the enolase N-terminal domain from Saccharomyces cerevisiae (PDB code 4enl ; residues 1–139; gray). The precorrin methyltransferase and enolase regions implicated in oligomerization and substrate binding are indicated.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| July 2010| Pages 1167-1173

doi:10.1107/S1744309110007517

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