 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](no5164fig1mag.jpg)
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Figure 1
Data for the crystal form in space group P2 are shown. (a) Overall structure of PhCheY with the protomers of a dimeric structure colored cyan and magenta. PhCheY retains the overall (β/α)5 fold of CheY, but shows a different packing by swapping about half of the fold. Three molecules are found in the asymmetric unit. Chain A is shown in cyan and the symmetry-related chain A′ is in magenta. The chains form a total interface of 2610 Å2 for the AA′ interaction (the values are 2460 Å2 for the BB′ interaction and 2420 Å2 for the CC′ interaction). (b) Superposition of the polypeptide chains within the asymmetric unit. The N-terminal parts of the chains (residues 1–53) have been superimposed. Superpositions were calculated with the LSQ tool (least-squares fit) in Coot (Emsley et al., 2010  ). (c) Superposition of PhCheY monomers (top; ribbon representation of backbone) and of a PhCheY pseudomonomer (reconstituted from chains A and A′) with T. maritima CheY (middle; PDB entry 1tmy; Usher et al., 1998). R.m.s.d. plot showing deviations from a chain A/A′ PhCheY pseudomonomer (bottom). Values were calculated with the SSM (secondary-structure match) tool in Coot (Emsley et al., 2010). The r.m.s.d. diagram shows the largest overall deviation in the β3–α3 loop hinge region (values exceeding 3 Å) as well as in the β5–α5 loop. (d) Topology diagram in the style of Fukami-Kobayashi et al. (1999) of the folds of CheY, the CheY homolog Spo0A and the evolutionarily related MglA. |
![[Figure 1]](no5164fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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