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 3
Metal coordination in Csd3_Δ41 and interactions of the C-terminal α-helix (α6) and β-strand (β22) with the core of domain 2. A ribbon diagram of the Csd3_Δ41 monomer, coloured as in Fig. 1

(a), is shown in the centre. The close-up views on the left represent interactions of the C-terminal strand (β22) with the β6 strand in the core of domain 2 (top) and of the C-terminal helix (α6) with the β-sheet in the core of domain 2 (bottom). Hydrogen-bond interactions are shown as black dotted lines. The close-up views on the right represent the ribbon diagram of the Zn²⁺-binding motif (top) and the surface representation of the substrate-binding groove formed by four loops of the LytM domain (bottom). The electron density for the Zn²⁺ ion in the OMIT mF_o − DF_c map is shown as a light pink mesh (contoured at 10σ). To show the detailed interactions more clearly, the close-up views have slightly different orientations.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

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

doi:10.1107/S1399004715000152

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