Structural basis for the inhibition of Mycobacterium tuberculosis l,d-transpeptidase by meropenem, a drug effective against extensively drug-resistant strains

Kim, H.S.; Kim, J.; Im, H.N.; Yoon, J.Y.; An, D.R.; Yoon, H.J.; Kim, J.Y.; Min, H.K.; Kim, S.-J.; Lee, J.Y.; Han, B.W.; Suh, S.W.

doi:10.1107/S0907444912048998

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 5
Conformational flexibility of the active-site lid in Ldt_Mt2Δ130. (a, b) Three different views of the electrostatic potential surface diagrams of mercury-derivatized (a) and meropenem-complexed Ldt_Mt2Δ130 (b). The closed conformation of the active-site lid in (b) reveals that meropem attached to catalytic Cys354 is accessible through three narrow paths (Paths A, B and C). (c) The active-site lids in meropenem-complexed (cyan) and mercury-derivatized (magenta) Ldt_Mt2Δ130 are shown as ribbon models with the surface of the meropenem complex. Residues that show large shifts upon lid closure are shown as stick models; the movement is indicated by black dotted arrows. The two models are in the same orientation.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 69| Part 3| February 2013| Pages 420-431

doi:10.1107/S0907444912048998

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