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 DSTRUCTURAL BIOLOGY

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Figure 2
Metal-dependency of H. pylori Csd4 as a carboxypeptidase. (a) Ribbon diagram of the active site in the Csd4-unbound structure coloured as in Fig. 1

(a). The OMIT mF_o − DF_c map (contoured at 5σ) for the calcium ion is coloured green. (b–e) Mass spectra of muramylpeptides after the reaction catalyzed by Csd4 in the presence of EDTA (b) or in the presence of Zn²⁺ (c), Ca²⁺ (d) or Mn²⁺ (e). Green and blue arrows indicate the peaks corresponding to the muramyldipeptide and muramyltripeptide (Tri), respectively.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S1399004714018732

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