Structure of the cystathionine γ-synthase MetB from Mycobacterium ulcerans

Clifton, M.C.; Abendroth, J.; Edwards, T.E.; Leibly, D.J.; Gillespie, A.K.; Ferrell, M.; Dieterich, S.H.; Exley, I.; Staker, B.L.; Myler, P.J.; Van Voorhis, W.C.; Stewart, L.J.

doi:10.1107/S1744309111029575

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
The active site of MetB covalently linked to PLP and bound to HEPES. The tight binding environment for the HEPES molecule is formed by a hydrogen-bonding network created by molecules of both monomers in the homodimer. Monomer A is indicated in blue, monomer B in yellow and HEPES in green; hydrogen bonds are represented by black dashed lines and range from 2.4 to 3.2 Å in length. The average B factors for the PLP and HEPES molecules in the MetB–PLP–HEPES structure are 9.1 and 15.9 Å², respectively.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 67| Part 9| August 2011| Pages 1154-1158

doi:10.1107/S1744309111029575

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