 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](tz5068fig1mag.jpg)
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Figure 1
Overall monomer structure and topology of H. pylori Csd3Δ41. (a) Ribbon diagram of the Csd3Δ41 monomer (chain A of form 1), with the secondary-structure elements labelled. Domain 1, the core of domain 2 and the LytM domain are shown in bright orange, sky blue and red, respectively. The C-terminal α-helix (α6) and β-strand (β22) are coloured teal. The green sphere is a Zn2+ ion. Side chains of the metal-coordinating residues (Glu74, His259, Asp263 and His341) are shown in stick models (dark grey). The secondary structures were defined by STRIDE (Heinig & Frishman, 2004  ). The walls of the active site in the LytM domain are made up of four loops: loop I (the β12–β13 loop), loop II (the β15–β16 loop), loop III (the β19–β20 loop) and loop IV (the β20–β21 loop). (b) Domains of H. pylori Csd3 coloured as in (a). TM, transmembrane helix. Residue numbers for each domain are indicated. (c) Topology diagram of Csd3Δ41 coloured as in (a). α-Helices, β-strands, 310-helices and loops are shown as cylinders, arrows, circles and solid lines, respectively. Structure figures were drawn using PyMOL (DeLano, 2002). |
![[Figure 1]](tz5068fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
