IPR001608
Alanine racemase, N-terminal
InterPro entry
Short name | Ala_racemase_N |
Overlapping homologous superfamilies |
Description
Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine.
The molecular structure of alanine racemase from Bacillus stearothermophilus was determined by X-ray crystallography to a resolution of 1.9 A
[1]. The alanine racemase monomer is composed of two domains, an eight-stranded α/β barrel at the N terminus, and a C-terminal domain essentially composed of β-strands. The pyridoxal 5'-phosphate (PLP) cofactor lies in and above the mouth of the α/β barrel and is covalently linked via an aldimine linkage to a lysine residue, which is at the C terminus of the first β-strand of the α/β barrel.
This N-terminal domain is also found in the PROSC (proline synthetase co-transcribed bacterial homologue) family of proteins, which are not known to have alanine racemase activity.
References
1.Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution. Shaw JP, Petsko GA, Ringe D. Biochemistry 36, 1329-42, (1997). View articlePMID: 9063881
Cross References
Contributing Member Database Entry
- Pfam:PF01168
Representative structure
1w8g: CRYSTAL STRUCTURE OF E. COLI K-12 YGGS