› 3m44

X-ray diffraction
1.4Å resolution

Crystal structure of the mutant V201A of orotidine 5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum

Released:
DOI: 10.2210/pdb3m44/pdb
PDB entry 3m44 coloured by chain, front view.
PDB entry 3m44 coloured by chain, side view.
PDB entry 3m44 coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus str. Delta H
Primary publication:
Conformational changes in orotidine 5'-monophosphate decarboxylase: "remote" residues that stabilize the active conformation.
Wood BM, Amyes TL, Fedorov AA, Fedorov EV, Shabila A, Almo SC, Richard JP, Gerlt JA
Biochemistry 49 3514-6 (2010)
PMID: 20369850

Function and Biology Details

Reaction catalysed: 
Orotidine 5'-phosphate = UMP + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127822 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Orotidine 5'-phosphate decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 228 amino acids
Theoretical weight: 24.86 KDa
Source organism: Methanothermobacter thermautotrophicus str. Delta H
Expression system: Escherichia coli
UniProt:
  • Canonical: O26232 (Residues: 1-228; Coverage: 100%)
Gene names: MTH_129, pyrF
Sequence domains: Orotidine 5'-phosphate decarboxylase / HUMPS family
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P212121
Unit cell:
a: 56.806Å b: 56.787Å c: 125.936Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.213 0.238
Expression system: Escherichia coli

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Citations

12 citation in other articles

Orotidine 5'-monophosphate decarboxylase: transition state stabilization from remote protein-phosphodianion interactions.
Amyes et al. (2012)
11 more