› 4fio

X-ray diffraction
1.37Å resolution

Crystal Structure of Methenyltetrahydromethanopterin Cyclohydrolase from Methanobrevibacter ruminantium

Released:
DOI: 10.2210/pdb4fio/pdb
PDB entry 4fio coloured by chain, front view.
PDB entry 4fio coloured by chain, side view.
PDB entry 4fio coloured by chain, top view.
Source organism: Methanobrevibacter ruminantium M1
Primary publication:
The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium.
Carbone V, Schofield LR, Beattie AK, Sutherland-Smith AJ, Ronimus RS
Proteins 81 2064-70 (2013)
PMID: 23873651

Function and Biology Details

Reaction catalysed: 
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H(2)O = 5-formyl-5,6,7,8-tetrahydromethanopterin
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112469 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methenyltetrahydromethanopterin cyclohydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 354 amino acids
Theoretical weight: 37.74 KDa
Source organism: Methanobrevibacter ruminantium M1
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: D3E4S5 (Residues: 1-321; Coverage: 100%)
Gene names: mch, mru_1619
Sequence domains: Cyclohydrolase (MCH)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand EEE 2 x EEE
Ligand IPA 3 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P1
Unit cell:
a: 52.37Å b: 74.855Å c: 74.816Å
α: 120.06° β: 100.01° γ: 98.28°
R-values:
R R work R free
0.132 0.13 0.175
Expression system: Escherichia coli BL21

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Citations

1 citations in other articles

RUMINANT NUTRITION SYMPOSIUM: Use of genomics and transcriptomics to identify strategies to lower ruminal methanogenesis.
McAllister et al. (2015)