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. Author manuscript; available in PMC: 2014 Sep 12.
Published in final edited form as: Proteins. 2008 Aug 15;72(3):848–862. doi: 10.1002/prot.21979

Table 2.

Residues involved in FNR:Fd interaction as experimentally determined by site-directed mutagenesis. Comparison with the experimental and theoretical structural models.

Intermolecular pairs a
NIP Anabaena x-ray Docking model b
FNR residuesc Fd residues a
 R16 (++)d 0.55 D67, D69, Q70 N9, E12, H16, G34, Y35, D36, L37, P38
 K72 (++)d 0.09 - E32
 K75 (++)e 0.28 S47, T48, E94, Y98 E24, D28, E31, E32
 L76 (++)f 0.40 A45, C46, F65, Y98 E31, D36, F39, R42
 L78 (++)f 0.58 A45, S64, F65, L66 E31, D36, F39, S40, C41, R42
 V136 (+)f 0.57 S64, F65, L66, D67, D68, Q70 D36, L37, P38, F39, S40, T48
 K138 (++)d 0.53 L66, D68 S40, S47, T48, H92, K93, E94, E95, Y98
 E139 (+)g,h,h 0.61 Q60, S61, D62, S64 S40, A45, C46, S47, T48, F65, E94, Y98, S2Fe2
 R264 (+)i 0.21 Y25, R42, A43, G44, D62, C79, V80 A43, D62
 K290 (+)d 0.25 - D67, D68
 K294 (++)d 0.28 - F65, D67, D69, Q70, L97, Y98
 E301 (+)i 0.48 S61, D62, Q63, S64 F39, S40, C41, A45, C46, T48
 T302 (+) k 0.50 A43, G44, D62, Q63, S64 S40, C41, R42, A43, A45
 Y303 (++)l 0.12 C41, A43, G44, A45, D62, Q63 S40, C41, A43
Fd residuesm FNR residuesa
 E32 (+)n 0.28 - K72, K75
 F39 (+)n 0.52 - N13, S59, I60, G61, L76, R77, L78, T133, V136, G137, E301, FAD
 S40 (+)o 0.53 FAD G57, S59, L78, V136, G137, K138, E139, M140, V300, E301, T302, Y303, FAD
 C41 (+)n 0.61 Y303, FAD L78, E267, V300, E301, T302, Y303, FAD
 R42 (+)p 0.49 R264 L76, L78, T302, FAD
 C46 (+)n 0.28 L76, FAD E139, V300, E301
 S47 (++)q 0.16 K75 K138, E139, V300
 T48 (+)o 0.19 K75 V136, G137, K138, E139, M140,
 D62 (+)q 0.24 E139, R264, E267, K293, V300, E301, T302, Y303 R264
 F65 (++)p 0.19 S59, L76, R77, L78, V136, FAD E139, K293, K294, W298, H299, V300
 D67 (+)r 0.02 V12, N13, R16, P135, V136 K290, D291, K293, K294
 D69 (+)r −0.12 V12, N13, R16 K294
 Q70 (+)q −0.06 N13, R16, V136 K294
 E94 (++)p 0.09 K75 G137, K138, E139, M140, L141
a

Two residues are considered to interact if any of their non-hydrogen atoms are at a distance ≤ 6 Å.

b

Docking model ranked 1 after rigid-body docking and refinement.

c

(++) Residues critically important for the interaction, when upon mutation the binding affinity changed at least one order of magnitude with respect to wild type, that is relative Kbind ≤0.1 or ≥10.0 as determined by difference spectroscopy; (+) Residues moderately important for the interaction, when upon mutation the binding affinity changed at least 20% with respect to wild type, that is relative Kbind ≤0.8 or ≥1.2; (−) Residues whose mutation does not affect the interaction (i.e. 0.8 < relative Kbind <1.2).

d

Data from Martínez-Júlvez et al. (1999).13

e

Data from Martínez-Júlvez et al. (1998).15

f

Data from Martínez-Júlvez et al. (2001).18

g

Data from Hurley et al. (2000).28

h

Data from Faro et al. (2002).38

i

Data from Martínez-Júlvez et al. (1998).14

j

Data from Medina et al. (1998).37

k

Data from Faro et al. (2002).40

l

Data from Nogues et al. (2004).39

m

(++) Residues critically important for the interaction, when upon mutation show relative kobs ≤0.1 or ≥10.0 as determined by laser flash photolysis; (+) Residues moderately important for the interaction, when relative kobs ≤0.8 or ≥1.2.

n

Data from Hurley et al. (2002).23

o

Data from Weber-Main et al. (1998).42

p

Data from Hurley et al. (1993).19

q

Data from Hurley et al. (1997).3

r

Data from Hurley et al. (1996).41