› 6jp9

X-ray diffraction
2.1Å resolution

Crsytal structure of a XMP complexed ATPPase subunit of M. jannaschii GMP synthetase

Released:
DOI: 10.2210/pdb6jp9/pdb
PDB entry 6jp9 coloured by chain, front view.
PDB entry 6jp9 coloured by chain, side view.
PDB entry 6jp9 coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii DSM 2661
Primary publication:
Mechanistic Insights into the Functioning of a Two-Subunit GMP Synthetase, an Allosterically Regulated, Ammonia Channeling Enzyme.
Shivakumaraswamy S, Kumar S, Bellur A, Polisetty SD, Balaram H
Biochemistry 61 1988-2006 (2022)
PMID: 36040251

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(4)(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176642 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP synthase [glutamine-hydrolyzing] subunit B Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 310 amino acids
Theoretical weight: 34.86 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q58531 (Residues: 1-310; Coverage: 100%)
Gene names: MJ1131, guaAB
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand XMP 4 x XMP
Ligand PGE 1 x PGE
Ligand MLA 1 x MLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 82.18Å b: 100.43Å c: 157.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.273
Expression system: Escherichia coli BL21(DE3)

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Citations

2 mentions without citation

GMP Synthetase: Allostery, Structure, and Function.
Ballut et al. (2023)
1 more