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 3
The interdomain pocket forms a unique catalytic site. (a) Surface representation of the Dhaf4260 domain interface colored by sequence conservation according to ConSurf (Landau et al., 2005

). High conservation among DUF364 homologs is indicated in maroon and low conservation is indicated in turquoise. A docked S-adenosyl-L-homocysteine (SAH) molecule is shown in ball-and-stick representation. Docking was based on its superposition with MT0146 (PDB code 1l3i ; Keller et al., 2002

). (b) Ribbon representation of Dhaf4260 in the same orientation as in (a). Highly conserved Dhaf4260 residues are shown in ball-and-stick representation and are labeled.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309110007517

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