› 1lm1

X-ray diffraction
2.8Å resolution

Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme

Released:
DOI: 10.2210/pdb1lm1/pdb
PDB entry 1lm1 coloured by chain, front view.
PDB entry 1lm1 coloured by chain, side view.
PDB entry 1lm1 coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6803
Primary publication:
Structural studies on the synchronization of catalytic centers in glutamate synthase.
van den Heuvel RH, Ferrari D, Bossi RT, Ravasio S, Curti B, Vanoni MA, Florencio FJ, Mattevi A
J Biol Chem 277 24579-83 (2002)
PMID: 11967268

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamate + NH(3) = L-glutamine + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferredoxin-dependent glutamate synthase 2 Chain: A
Molecule details ›
Chain: A
Length: 1520 amino acids
Theoretical weight: 165.71 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli
UniProt:
  • Canonical: P55038 (Residues: 37-1556; Coverage: 98%)
Gene names: gltS, sll1499
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
2 bound ligands:
Ligand ACT 2 x ACT
Ligand F3S 1 x F3S
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P43212
Unit cell:
a: 166.083Å b: 166.083Å c: 219.584Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.236 0.287
Expression system: Escherichia coli

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Citations

13 review citations

Investigation of intact protein complexes by mass spectrometry.
Heck et al. (2004)
12 more

2 mentions without citation

Crystal structure of a major secreted protein of Mycobacterium tuberculosis-MPT63 at 1.5-A resolution.
Goulding et al. (2002)
1 more