Magnesium in PDB 8qmv: L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos
Enzymatic activity of L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos
All present enzymatic activity of L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos:
4.1.1.39;
Protein crystallography data
The structure of L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos, PDB code: 8qmv
was solved by
J.Zarzycki,
L.Schulz,
T.J.Erb,
G.K.A.Hochberg,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
24.97 /
1.85
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
121.79,
203.8,
147.37,
90,
90,
90
|
R / Rfree (%)
|
16.1 /
17.4
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos
(pdb code 8qmv). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos, PDB code: 8qmv:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 8qmv
Go back to
Magnesium Binding Sites List in 8qmv
Magnesium binding site 1 out
of 4 in the L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg502
b:23.2
occ:1.00
|
OD1
|
A:ASP189
|
2.0
|
21.9
|
1.0
|
OQ2
|
A:KCX187
|
2.0
|
20.8
|
1.0
|
O6
|
A:CAP501
|
2.1
|
20.2
|
1.0
|
OE1
|
A:GLU190
|
2.1
|
21.2
|
1.0
|
O3
|
A:CAP501
|
2.2
|
20.7
|
1.0
|
O2
|
A:CAP501
|
2.3
|
21.7
|
1.0
|
C
|
A:CAP501
|
2.8
|
21.9
|
1.0
|
C2
|
A:CAP501
|
2.9
|
20.8
|
1.0
|
CX
|
A:KCX187
|
3.0
|
21.5
|
1.0
|
C3
|
A:CAP501
|
3.1
|
19.4
|
1.0
|
CD
|
A:GLU190
|
3.1
|
21.6
|
1.0
|
CG
|
A:ASP189
|
3.2
|
21.3
|
1.0
|
OQ1
|
A:KCX187
|
3.4
|
21.3
|
1.0
|
OE2
|
A:GLU190
|
3.6
|
21.0
|
1.0
|
NZ
|
A:LYS163
|
3.7
|
21.0
|
1.0
|
ND2
|
B:ASN109
|
3.8
|
20.8
|
1.0
|
N
|
A:GLU190
|
3.8
|
20.4
|
1.0
|
CG2
|
A:THR159
|
3.9
|
20.2
|
1.0
|
OD2
|
A:ASP189
|
3.9
|
21.0
|
1.0
|
NZ
|
A:LYS161
|
4.0
|
21.1
|
1.0
|
O7
|
A:CAP501
|
4.0
|
21.5
|
1.0
|
CA
|
A:ASP189
|
4.0
|
19.4
|
1.0
|
NE2
|
A:HIS280
|
4.1
|
20.6
|
1.0
|
CB
|
A:ASP189
|
4.1
|
20.6
|
1.0
|
NZ
|
A:KCX187
|
4.2
|
19.4
|
1.0
|
OG1
|
A:THR159
|
4.3
|
21.4
|
1.0
|
C4
|
A:CAP501
|
4.3
|
20.6
|
1.0
|
C1
|
A:CAP501
|
4.3
|
20.6
|
1.0
|
CG
|
A:GLU190
|
4.4
|
20.2
|
1.0
|
C
|
A:ASP189
|
4.5
|
19.7
|
1.0
|
CB
|
A:THR159
|
4.6
|
23.2
|
1.0
|
CB
|
A:GLU190
|
4.6
|
19.8
|
1.0
|
O1
|
A:CAP501
|
4.7
|
21.5
|
1.0
|
CD2
|
A:HIS280
|
4.7
|
19.1
|
1.0
|
C5
|
A:CAP501
|
4.8
|
19.3
|
1.0
|
CA
|
A:GLU190
|
4.9
|
20.5
|
1.0
|
O
|
B:HOH681
|
4.9
|
21.8
|
1.0
|
CE1
|
A:HIS280
|
4.9
|
19.8
|
1.0
|
CG
|
B:ASN109
|
5.0
|
23.1
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 8qmv
Go back to
Magnesium Binding Sites List in 8qmv
Magnesium binding site 2 out
of 4 in the L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg502
b:23.2
occ:1.00
|
OD1
|
B:ASP189
|
2.0
|
21.2
|
1.0
|
OQ1
|
B:KCX187
|
2.0
|
20.4
|
1.0
|
OE1
|
B:GLU190
|
2.1
|
22.5
|
1.0
|
O6
|
B:CAP501
|
2.1
|
22.2
|
1.0
|
O3
|
B:CAP501
|
2.2
|
22.4
|
1.0
|
O2
|
B:CAP501
|
2.3
|
20.7
|
1.0
|
C2
|
B:CAP501
|
2.8
|
22.1
|
1.0
|
C
|
B:CAP501
|
2.9
|
23.8
|
1.0
|
CX
|
B:KCX187
|
3.0
|
22.7
|
1.0
|
C3
|
B:CAP501
|
3.0
|
21.6
|
1.0
|
CD
|
B:GLU190
|
3.1
|
23.7
|
1.0
|
CG
|
B:ASP189
|
3.2
|
23.0
|
1.0
|
OQ2
|
B:KCX187
|
3.3
|
22.3
|
1.0
|
OE2
|
B:GLU190
|
3.6
|
24.1
|
1.0
|
ND2
|
A:ASN109
|
3.8
|
22.2
|
1.0
|
NZ
|
B:LYS163
|
3.8
|
21.6
|
1.0
|
N
|
B:GLU190
|
3.8
|
20.8
|
1.0
|
NZ
|
B:LYS161
|
3.9
|
20.5
|
1.0
|
OD2
|
B:ASP189
|
3.9
|
23.6
|
1.0
|
CG2
|
B:THR159
|
4.0
|
22.5
|
1.0
|
NE2
|
B:HIS280
|
4.0
|
20.3
|
1.0
|
CA
|
B:ASP189
|
4.1
|
21.8
|
1.0
|
O7
|
B:CAP501
|
4.1
|
24.0
|
1.0
|
CB
|
B:ASP189
|
4.1
|
21.8
|
1.0
|
NZ
|
B:KCX187
|
4.2
|
20.9
|
1.0
|
OG1
|
B:THR159
|
4.3
|
22.4
|
1.0
|
C4
|
B:CAP501
|
4.3
|
23.1
|
1.0
|
C1
|
B:CAP501
|
4.3
|
23.0
|
1.0
|
CG
|
B:GLU190
|
4.4
|
20.2
|
1.0
|
C
|
B:ASP189
|
4.5
|
21.1
|
1.0
|
CB
|
B:GLU190
|
4.6
|
20.1
|
1.0
|
CB
|
B:THR159
|
4.6
|
22.2
|
1.0
|
CD2
|
B:HIS280
|
4.7
|
20.1
|
1.0
|
O1
|
B:CAP501
|
4.7
|
23.2
|
1.0
|
C5
|
B:CAP501
|
4.8
|
23.3
|
1.0
|
CA
|
B:GLU190
|
4.8
|
19.5
|
1.0
|
CE1
|
B:HIS280
|
4.9
|
22.7
|
1.0
|
CG
|
A:ASN109
|
5.0
|
23.2
|
1.0
|
O
|
A:HOH659
|
5.0
|
25.5
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 8qmv
Go back to
Magnesium Binding Sites List in 8qmv
Magnesium binding site 3 out
of 4 in the L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg502
b:25.5
occ:1.00
|
OE1
|
C:GLU190
|
2.0
|
24.5
|
1.0
|
OD1
|
C:ASP189
|
2.1
|
26.5
|
1.0
|
O6
|
C:CAP501
|
2.1
|
25.8
|
1.0
|
OQ1
|
C:KCX187
|
2.1
|
23.9
|
1.0
|
O3
|
C:CAP501
|
2.2
|
23.5
|
1.0
|
O2
|
C:CAP501
|
2.3
|
24.6
|
1.0
|
C
|
C:CAP501
|
2.8
|
25.8
|
1.0
|
C2
|
C:CAP501
|
2.8
|
23.7
|
1.0
|
C3
|
C:CAP501
|
3.0
|
23.8
|
1.0
|
CX
|
C:KCX187
|
3.0
|
25.2
|
1.0
|
CD
|
C:GLU190
|
3.1
|
24.2
|
1.0
|
CG
|
C:ASP189
|
3.3
|
26.7
|
1.0
|
OQ2
|
C:KCX187
|
3.3
|
25.9
|
1.0
|
OE2
|
C:GLU190
|
3.5
|
24.1
|
1.0
|
ND2
|
D:ASN109
|
3.7
|
24.4
|
1.0
|
NZ
|
C:LYS163
|
3.8
|
27.1
|
1.0
|
N
|
C:GLU190
|
3.8
|
23.1
|
1.0
|
NE2
|
C:HIS280
|
4.0
|
22.0
|
1.0
|
NZ
|
C:LYS161
|
4.0
|
26.4
|
1.0
|
O7
|
C:CAP501
|
4.0
|
25.3
|
1.0
|
OD2
|
C:ASP189
|
4.1
|
26.6
|
1.0
|
CG2
|
C:THR159
|
4.1
|
24.6
|
1.0
|
CA
|
C:ASP189
|
4.1
|
23.8
|
1.0
|
CB
|
C:ASP189
|
4.2
|
22.8
|
1.0
|
NZ
|
C:KCX187
|
4.2
|
23.1
|
1.0
|
C4
|
C:CAP501
|
4.3
|
23.6
|
1.0
|
OG1
|
C:THR159
|
4.3
|
25.6
|
1.0
|
C1
|
C:CAP501
|
4.3
|
23.9
|
1.0
|
CG
|
C:GLU190
|
4.4
|
21.5
|
1.0
|
C
|
C:ASP189
|
4.5
|
23.7
|
1.0
|
CB
|
C:GLU190
|
4.6
|
22.0
|
1.0
|
CD2
|
C:HIS280
|
4.6
|
23.9
|
1.0
|
CB
|
C:THR159
|
4.7
|
24.6
|
1.0
|
O1
|
C:CAP501
|
4.7
|
23.7
|
1.0
|
C5
|
C:CAP501
|
4.7
|
23.0
|
1.0
|
CA
|
C:GLU190
|
4.8
|
22.6
|
1.0
|
O
|
D:HOH697
|
4.9
|
26.6
|
1.0
|
CE1
|
C:HIS280
|
4.9
|
23.4
|
1.0
|
CG
|
D:ASN109
|
4.9
|
27.3
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 8qmv
Go back to
Magnesium Binding Sites List in 8qmv
Magnesium binding site 4 out
of 4 in the L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of L2 Forming Rubisco Derived From Ancestral Sequence Reconstruction of the Last Common Ancestor of Form I'' and Form I Rubiscos within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg502
b:23.1
occ:1.00
|
OE1
|
D:GLU190
|
2.0
|
23.0
|
1.0
|
OD1
|
D:ASP189
|
2.0
|
23.9
|
1.0
|
O6
|
D:CAP501
|
2.1
|
21.0
|
1.0
|
OQ2
|
D:KCX187
|
2.1
|
22.2
|
1.0
|
O3
|
D:CAP501
|
2.2
|
20.9
|
1.0
|
O2
|
D:CAP501
|
2.3
|
22.4
|
1.0
|
C
|
D:CAP501
|
2.8
|
23.2
|
1.0
|
C2
|
D:CAP501
|
2.8
|
22.7
|
1.0
|
C3
|
D:CAP501
|
3.0
|
22.0
|
1.0
|
CD
|
D:GLU190
|
3.0
|
23.2
|
1.0
|
CX
|
D:KCX187
|
3.1
|
23.1
|
1.0
|
CG
|
D:ASP189
|
3.2
|
24.1
|
1.0
|
OQ1
|
D:KCX187
|
3.4
|
24.4
|
1.0
|
OE2
|
D:GLU190
|
3.5
|
22.3
|
1.0
|
ND2
|
C:ASN109
|
3.7
|
21.5
|
1.0
|
NZ
|
D:LYS163
|
3.7
|
23.4
|
1.0
|
N
|
D:GLU190
|
3.8
|
20.1
|
1.0
|
OD2
|
D:ASP189
|
4.0
|
24.6
|
1.0
|
NZ
|
D:LYS161
|
4.0
|
21.1
|
1.0
|
CG2
|
D:THR159
|
4.0
|
21.4
|
1.0
|
NE2
|
D:HIS280
|
4.0
|
21.4
|
1.0
|
O7
|
D:CAP501
|
4.0
|
21.3
|
1.0
|
CA
|
D:ASP189
|
4.1
|
21.5
|
1.0
|
CB
|
D:ASP189
|
4.1
|
22.4
|
1.0
|
NZ
|
D:KCX187
|
4.3
|
21.1
|
1.0
|
C4
|
D:CAP501
|
4.3
|
22.3
|
1.0
|
CG
|
D:GLU190
|
4.3
|
21.1
|
1.0
|
OG1
|
D:THR159
|
4.3
|
22.0
|
1.0
|
C1
|
D:CAP501
|
4.3
|
24.9
|
1.0
|
C
|
D:ASP189
|
4.5
|
21.6
|
1.0
|
CB
|
D:GLU190
|
4.5
|
19.7
|
1.0
|
CD2
|
D:HIS280
|
4.7
|
20.2
|
1.0
|
CB
|
D:THR159
|
4.7
|
21.4
|
1.0
|
C5
|
D:CAP501
|
4.7
|
21.0
|
1.0
|
O1
|
D:CAP501
|
4.7
|
23.5
|
1.0
|
CA
|
D:GLU190
|
4.8
|
20.7
|
1.0
|
CG
|
C:ASN109
|
4.9
|
23.1
|
1.0
|
O
|
C:HOH667
|
4.9
|
25.7
|
1.0
|
CE1
|
D:HIS280
|
4.9
|
20.1
|
1.0
|
|
Reference:
L.Schulz,
J.Zarzycki,
W.Steinchen,
G.K.A.Hochberg,
T.J.Erb.
Layered Entrenchment Maintains Essentiality in the Evolution of Form I Rubisco Complexes Biorxiv 2024.
ISSN: ISSN 2692-8205
DOI: 10.1101/2024.01.18.576253
Page generated: Thu Oct 31 21:59:11 2024
|