Structural basis for the recognition of muramyltripeptide by Helicobacter pylori Csd4, a d,l-carboxypeptidase controlling the helical cell shape

Kim, H.S.; Kim, J.; Im, H.N.; An, D.R.; Lee, M.; Hesek, D.; Mobashery, S.; Kim, J.Y.; Cho, K.; Yoon, H.J.; Han, B.W.; Lee, B.I.; Suh, S.W.

doi:10.1107/S1399004714018732

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 5
Open and closed conformations of the flap. Electrostatic surface diagrams of the mobile flap (left panels) and surface diagrams showing the active-site cleft (right panels) in the Csd4-unbound (a), Csd4–muramyltripeptide (b) and Csd4–mDAP (c) structures.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 70| Part 11| November 2014| Pages 2800-2812

https://doi.org/10.1107/S1399004714018732

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