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. Author manuscript; available in PMC: 2019 Jun 5.
Published in final edited form as: Biochemistry. 2018 Apr 13;57(22):3134–3145. doi: 10.1021/acs.biochem.8b00092

Figure 7.

Figure 7.

PMP active site at pH 8.0. (A) Active site of yCBS-cc after soaking with hydrazine. Fobs – Fcalc electron density contoured at 3σ from a simulated annealing omit map is shown in green. K53 is shifted away from PMP. Acetate does not appear to be present in this active site; a water molecule is bound instead (WA). (B) K53 is shifted away from its internal aldimine position and interacts with a water molecule that is held in place by surrounding residues. This latter water is also present in the other active-site structures reported here (Figures 4 and 5) and interacts with K53 in all of the external aldimine intermediate structures (Figure 5). Atoms are colored according to element as follows: magenta, carbon; blue, nitrogen; red, oxygen; orange, phosphorus. The carbon atoms of PLP are colored yellow.