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![[Figure 1]](cb5035fig1mag.jpg)
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Figure 1
Tetrameric structure of PYK and the disposition of domains. (a) The four polypeptide chains of TbPYK–F26BP–PEP–Mg. The large (A–A) and small (C–C) interfaces are indicated by dashed lines and the active and effector sites are boxed. Chain A shows the N-terminal domain (green; residues 2–18), A domain (yellow; residues 19–89 and 188–358), B domain (blue; residues 90–187) and C domain (red; residues 359–499). (b) An overlay of the AC domains from three PYK crystal structures: TbPYK–F26BP–Mg (pink), TbPYK–F26BP–PEP–Mg (blue) and LmPYK–F26BP–OX–ATP–Mg (black; PDB entry 3hqp). The B-domain rotations of these PYK complexes were analysed using DynDom (Hayward et al., 1997  ; Hayward & Berendsen, 1998). The B domain in TbPYK–F26BP–Mg is in the open conformation, while the B domain in TbPYK–F26BP–PEP–Mg is in the partially or half-closed conformation. LmPYK–F26BP–OX–ATP–Mg has the B domain in its fully closed position. |
![[Figure 1]](cb5035fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
