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. 2006 Aug;188(16):6020–6025. doi: 10.1128/JB.00379-06

FIG. 4.

FIG. 4.

(a) Comparison of the growth of wild-type A. vinelandii (WT) with that of nifM A. vinelandii BG98 and its derivatives carrying pBG3605 (p258S mutant), pBG3601 (P232K P258S double mutant), or pBG3609 (P232K mutation alone) on a BN− agar plate. All strains were plated on a BN+ agar plate and a BN−agar plate and incubated at 30°C for 72 h. On the BN− agar plate, the growth of wild-type A. vinelandii was comparable to the growth of nifM A. vinelandii BG98 carrying the plasmid pBG3601 or pBG3605. Neither nifM A. vinelandii BG98 nor its derivative carrying pBG3609 could grow on BN− agar plates. (b) Ribbon diagram of the Av2 dimer (Protein Data Bank code 2NIP) (27). The location of P258 (marked by the arrow) is in the C-terminal region of the NifH subunit, which wraps around the other subunit of the NifH dimer. It is conceivable that the structure of this region, caused by the specific conformation of the rigid peptidyl-prolyl bond (presumably converted to trans conformation by NifM) of P258, plays a significant role in the folding of NifH to generate a functional molecule.