Structure of Csd3 from Helicobacter pylori, a cell shape-determining metallopeptidase

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

doi:10.1107/S1399004715000152

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 5
Conserved residues in the active site of M23B metallopeptidases. (a) Superposition of LytM domains in two crystal forms of H. pylori Csd3. Chain A of the form 1 crystal (red) and the form 2 crystal (pink) are shown as ribbon diagrams. (b) Superposition of the LytM domains in two M23B family members (NMB0315 and VC0503) coloured as in Fig. 4

(b). Conserved residues are shown as stick models and are labelled (NMB0315 at the top and VC0503 at the bottom). Metal ions and water molecules are shown as green spheres and blue dots, respectively. In NMB0315, the Zn²⁺ ion was replaced by an Ni²⁺ ion during affinity chromatography (Wang et al., 2011

). Wat-1 and Wat-2 are present in NMB0315, where the Ni²⁺ ion is pentacoordinated. Black dotted lines denote hydrogen bonds to Wat-1 in NMB0315. In VC0503, the Zn²⁺ ion is tetracoordinated, with one water molecule (omitted for clarity) located between Wat-1 and Wat-2.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 71| Part 3| February 2015| Pages 675-686

doi:10.1107/S1399004715000152

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