ID Card:
Full name:
Ribosomal RNA small subunit methyltransferase G
Synonym:
gidB
GI:
121190
COG:
COG0357
UniProt:
P25813
Structures:
|
1XDZ |
Alpha Fold Predicted Structure:
AF-P25813-F1
Enzyme type:
methyltransferase
Position of modification - modification:
s :533(527) - m7G
PDB Structures:
1XDZ
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1XDZ
Structure Description:
Title:
Crystal Structure of Gram_Positive Bacillus subtilis Glucose inhibited Division protein B (gidB), Structural genomics, MCSG
Classification:
TRANSFERASE
X-Ray Diffraction
1.6
0.221
0.203
0.202
Abstract of the PDB Structure's related Publication:
Download RCSB-PDB Structures:
Protein sequence:
MNIEEFTSGLAEKGISLSPRQLEQFELYYDMLVEWNEKINLTSITEKKEVYLKHFYDSITAAFYVDFNQVNTICDVGAGAGFPSLPIKICFPHLHVTIVDSLNKRITFLEKLSEALQLENTTFCHDRAETFGQRKDVRESYDIVTARAVARLSVLSELCLPLVKKNGLFVALKAASAEEELNAGKKAITTLGGELENIHSFKLPIEESDRNIMVIRKIKNTPKKYPRKPGTPNKSPIEG
Comments:
RsmG is responsible for the synthesis of m7G535 (position 527 in E. coli) in the universally conserved loop of hairpin 18 in domain I. This modified nucleotide plays an essential role in binding antibiotics like streptomycin and kasugamycin. However the dependence on RsmG for antibiotic binding depends on the activity of RsmA (KsgA) catalyzing the formation of m6,6A1518,1519 at the 3'-end of 16S rRNA by RsmA (KsgA). In B. subtilis, mutations in both RsmA and RsmG allow better cell viability in the presence of antibiotics. AdoMet is the methyl group donor.
Alpha Fold Predicted Structure:
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Protein sequence:
M
N
I
E
E
F
T
S
G
L
A
E
K
G
I
S
L
S
P
R
Q
L
E
Q
F
E
L
Y
Y
D
M
L
V
E
W
N
E
K
I
N
L
T
S
I
T
E
K
K
E
V
Y
L
K
H
F
Y
D
S
I
T
A
A
F
Y
V
D
F
N
Q
V
N
T
I
C
D
V
G
A
G
A
G
F
P
S
L
P
I
K
I
C
F
P
H
L
H
V
T
I
V
D
S
L
N
K
R
I
T
F
L
E
K
L
S
E
A
L
Q
L
E
N
T
T
F
C
H
D
R
A
E
T
F
G
Q
R
K
D
V
R
E
S
Y
D
I
V
T
A
R
A
V
A
R
L
S
V
L
S
E
L
C
L
P
L
V
K
K
N
G
L
F
V
A
L
K
A
A
S
A
E
E
E
L
N
A
G
K
K
A
I
T
T
L
G
G
E
L
E
N
I
H
S
F
K
L
P
I
E
E
S
D
R
N
I
M
V
I
R
K
I
K
N
T
P
K
K
Y
P
R
K
P
G
T
P
N
K
S
P
I
E
G
20 40 60 80 100 120 140 160 180 200 220 Sequence G H I T S N
Secondary Structure Alphabet
G: 3-turn helix (310 helix) H: α-helix I: 𝝅-helix (5 - turn helix) T: Hydrogen Bonded Turn B: β-sheet S: Bend C: Coil (residues not present in any of the above conformations) N: Not assigned
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Publications: