Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism

Bakolitsa, C.; Kumar, A.; Jin, K.K.; McMullan, D.; Krishna, S.S.; Miller, M.D.; Abdubek, P.; Acosta, C.; Astakhova, T.; Axelrod, H.L.; Burra, P.; Carlton, D.; Chen, C.; Chiu, H.-J.; Clayton, T.; Das, D.; Deller, M.C.; Duan, L.; Elias, Y.; Ellrott, K.; Ernst, D.; Farr, C.L.; Feuerhelm, J.; Grant, J.C.; Grzechnik, A.; Grzechnik, S.K.; Han, G.W.; Jaroszewski, L.; Johnson, H.A.; Klock, H.E.; Knuth, M.W.; Kozbial, P.; Marciano, D.; Morse, A.T.; Murphy, K.D.; Nigoghossian, E.; Nopakun, A.; Okach, L.; Paulsen, J.; Puckett, C.; Reyes, R.; Rife, C.L.; Sefcovic, N.; Tien, H.J.; Trame, C.B.; Trout, C.V.; van den Bedem, H.; Weekes, D.; White, A.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Elsliger, M.-A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.

doi:10.1107/S1744309109050647

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Oligomerization states of BB2672 and monofunctional BCM. (a) Ribbon diagram of the BB2672 hexamer showing the arrangement of consecutive subunits (top view). The three molecules present in the asymmetric unit are labeled A, B and C in red. A′, B′ and C′ are the corresponding crystallographically related molecules that together form the BB2672 hexamer. Protomers with their N-terminus pointing to the front are shown in gray and those with their N-terminus pointing towards the back are shown in blue. The C-terminal `dimer' interface occurs between protomers B–C, B′–C′ and A–A′. The N-terminal interface occurs between protomers A–B, A′–B′ and C–C′. (b) Ribbon diagram of the BCM trimer (PDB code 2cht , top view) showing the parallel arrangement of protomers resulting in three equivalent interfaces.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| March 2010| Pages 1182-1189

doi:10.1107/S1744309109050647

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