Table 3 Binding affinities of LysM alanine mutants determined by SPR.

From: Molecular basis for bacterial peptidoglycan recognition by LysM domains

LysM

K D (μM)

Residual binding (%)

WT

11.7±1.7

100

D12A

72.0±15.2

16.2

T13A

730.2±83.1

1.6 (17.1)

L14A

927.9±151.1

1.3

N15A

21.5±3.9

64.1 (50.0)

K16A

13.1±1.2

89.3

N32A

15.8±2.3

74.0

D37A

138.3±14.2

10.0

L38A

145.5±27.7

12.4 (28.9)

I39A

1,021±224.2

1.3 (1.6)

F40A

54.0±12.0

25.5 (29.7)

V41A

11.7±2.1

100.0 (50.1)

  1. GlcNAc5 was used as the analyte. Residual activity is the ratio of the apparent affinity to that of wild-type, obtained from surface plasmon resonance (SPR) or NMR (NMR values in brackets).
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