Conformational changes associated with the binding of zinc acetate at the putative active site of XcTcmJ, a cupin from Xanthomonas campestris pv. campestris

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

doi:10.1107/S1744309109021988

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
Stereo diagram of residues in the putative active site of XcTcmJ from X. campestris pv. campestris. The C, O, N and Se (from selenomethionine) atoms of the side chains of XcTcmJ and the bound acetate ligand (labeled ACT) are shown in green, red, blue and orange, respectively. The bound Zn atom and water molecules are shown as orange and red spheres, respectively. His41, Gln46 and His80, which are within coordination distance of the bound zinc, are labeled in italics.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| October 2010| Pages 1347-1353

doi:10.1107/S1744309109021988

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