› 4m7s

X-ray diffraction
2.02Å resolution

Crystal structure of SeMet BtrN in an OPEN conformation

Released:
DOI: 10.2210/pdb4m7s/pdb
PDB entry 4m7s coloured by chain, front view.
PDB entry 4m7s coloured by chain, side view.
PDB entry 4m7s coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry.
Goldman PJ, Grove TL, Booker SJ, Drennan CL
Proc Natl Acad Sci U S A 110 15949-54 (2013)
PMID: 24048029

Function and Biology Details

Reaction catalysed: 
2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine = 3-amino-2,3-dideoxy-scyllo-inosose + 5'-deoxyadenosine + L-methionine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-568512 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosyl-L-methionine-dependent 2-deoxy-scyllo-inosamine dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 31.08 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8G907 (Residues: 1-250; Coverage: 100%)
Gene name: btrN
Sequence domains:
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand SF4 2 x SF4
Ligand GOL 2 x GOL
Ligand IMD 1 x IMD
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 99.408Å b: 42.058Å c: 50.925Å
α: 90° β: 105.4° γ: 90°
R-values:
R R work R free
0.173 0.171 0.218
Expression system: Escherichia coli

Quick links

Citations

16 review citations

SPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymes.
Grell et al. (2015)
15 more

2 mentions without citation

X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry.
Goldman et al. (2013)
1 more