› 7x5o

X-ray diffraction
2.62Å resolution

Crystal structure of E. faecium SHMT in complex with Me-THF and PLP-Gly

Released:
DOI: 10.2210/pdb7x5o/pdb
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PDB entry 7x5o coloured by chain, front view.
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Source organism: Enterococcus faecium
Primary publication:
Serine hydroxymethyltransferase as a potential target of antibacterial agents acting synergistically with one-carbon metabolism-related inhibitors.
Makino Y, Oe C, Iwama K, Suzuki S, Nishiyama A, Hasegawa K, Okuda H, Hirata K, Ueno M, Kawaji K, Sasano M, Usui E, Hosaka T, Yabuki Y, Shirouzu M, Katsumi M, Murayama K, Hayashi H, Kodama EN
OpenAccess logo Commun Biol 5 619 (2022)
PMID: 35739195

Function and Biology Details

Reaction catalysed: 
5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125092 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 417 amino acids
Theoretical weight: 45.01 KDa
Source organism: Enterococcus faecium
Expression system: Escherichia coli
UniProt:
  • Canonical: I3U4H4 (Residues: 1-414; Coverage: 100%)
Gene names: HMPREF0351_12288, glyA
Sequence domains: Serine hydroxymethyltransferase

Ligands and Environments


Cofactor: Ligand THH 3 x THH
1 bound ligand:
Ligand PLG 2 x PLG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P41212
Unit cell:
a: 126.981Å b: 126.981Å c: 170.106Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.154 0.194
Expression system: Escherichia coli

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Citations

3 citation in other articles

Enhanced Antibacterial Activity of Substituted Derivatives of NCR169C Peptide.
Howan et al. (2023)
2 more

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