 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](no5164fig2mag.jpg)
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Figure 2
Comparative analysis of CheY. (a) Superposition of the PhCheY pseudomonomer (reconstituted from chains A and A′) with M. maripaludis CheY (PDB entries 6ekg and 6ekh; Quax, Altegoer et al., 2018  ). Views and arrangement are as in Fig. 1(c). Superpositions were calculated with the LSQ tool (least-squares fit) in Coot (Emsley et al., 2010). PhCheY is in magenta/cyan and BeF3−/NaF-activated and non-activated M. maripaludis CheY are in orange and yellow, respectively. The gray background refers to (b). (b) Enlargement of the CheY structures in the orientations indicated in (a). Residues Asp53/Asp57 (P. horikoshi/M. maripaludis numbering), Tyr100/Tyr104 and Thr81/Thr84 are shown in stick representation using the color code in (a). (c) Qualitative surface electrostatic representation of CheY from P. horikoshi, M. maripaludis and T. maritima (PDB entry 1tmy; Usher et al., 1998) calculated with the vacuum electrostatics function in PyMOL (http://www.pymol.org) and shown in default coloring with positive potentials depicted in blue and negative potentials in red. The α4 helices including the positions of Gln85 and Glu86 (P. horikoshi numbering; Glu89 and Gln90 in M. maripaludis) are circled in yellow. (d) Sequence alignment in P. horikoshi numbering generated with Clustal Omega (Thompson et al., 1997) and rendered in Jalview (Waterhouse et al., 2009). |
![[Figure 2]](no5164fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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