Table 1 Functional contribution of sectors defined for the ptRNase superfamily.

From: Conserved amino acid networks modulate discrete functional properties in an enzyme superfamily

IC

Residue mapping on 3D structure

Residue

Function

Reference

1

C26

Stabilizing the conformation (S-S bond with C84)

32

C40

Stabilizing the conformation (S-S bond with C95)

32

F46

Chain folding initiation site (CFIS) residue

33

C58

Stabilizing the conformation (S-S bond with C110)

32

S75

H-bonding with I106, Hydrophobic core

34

C84

Stabilizing the conformation (S-S bond with C84)

32

C95

Stabilizing the conformation (S-S bond with C40)

32

Y97

CFIS residue (fixes K41 through H-bonding)

12, 35

C110

Stabilizing the conformation (S-S bond with C58)

32

2

K7

P2 substrate binding site for endonuclease specificity

35

R10

P2 substrate binding site for endonuclease specificity

35

D14

H-bonding with Y25

36

Y25

Hydrophobic core, H-bonding with D14

36

M29

Hydrophobic core

37, 38

R33

H-bonding with R10 and M13

39

N34

Part of N-glycosylation sequence (N34-L35-T36)

40

T36

Part of N-glycosylation sequence(N34-L35-T36)

40

V47

Hydrophobic core

38

L51

Hydrophobic core

38

I106

Hydrophobic core, expedites folding

34

F120

Hydrophobic core, fixes the side-chain of H119

34

3

F8

Juxtaposing His12 by π-interaction with His12

35

Q11

P1 substrate binding site

35

H12

Catalytic triad residue (General base for catalysis)

34

M30

Hydrophobic core

38

K41

Catalytic triad residue (H-bond with transition state)

37

N44

H-bonding with H12 and K41

34

T45

Pyrimidine specificity of the B1 site

35

N71

B2 substrate binding site

35

A109

CFIS residue

35

P117

Trans-isomerization for folding

35

V118

CFIS residue

35

H119

Catalytic triad residue (General acid for catalysis)

34

D121

P1 substrate binding site

35

  1. Amino acid residues of each ICs are represented using the space filling model and mapped on the 3D structure of bovine RNase A (PDB 7RSA).