TY  - JOUR
A1  - Varshney, Nishant Kumar
A1  - Kumar, R. Suresh
A1  - Ignatova, Zoya
A1  - Prabhune, Asmita
A1  - Pundle, Archana
A1  - Dodson, Eleanor
A1  - Suresh, C. G.
T1  - Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis
JF  - Acta crystallographica : Section F, Structural biology communications
N2  - The enzyme penicillin G acylase (EC 3.5.1.11) catalyzes amide-bond cleavage in benzylpenicillin (penicillin G) to yield 6-aminopenicillanic acid, an intermediate chemical used in the production of semisynthetic penicillins. A thermostable penicillin G acylase from Alcaligenes faecalis (AfPGA) has been crystallized using the hanging-drop vapour-diffusion method in two different space groups: C2221, with unit-cell parameters a = 72.9, b = 86.0, c = 260.2 angstrom, and P41212, with unit-cell parameters a = b = 85.6, c = 298.8 angstrom. Data were collected at 293 K and the structure was determined using the molecular-replacement method. Like other penicillin acylases, AfPGA belongs to the N-terminal nucleophilic hydrolase superfamily, has undergone post-translational processing and has a serine as the N-terminal residue of the beta-chain. A disulfide bridge has been identified in the structure that was not found in the other two known penicillin G acylase structures. The presence of the disulfide bridge is perceived to be one factor that confers higher stability to this enzyme.
KW  - thermostability
KW  - disulfide bridges
KW  - Ntn hydrolases
KW  - orthorhombic form
KW  - tetragonal form
KW  - calcium binding
Y1  - 2012
U6  - https://doi.org/10.1107/S1744309111053930
SN  - 1744-3091
VL  - 68
IS  - 3
SP  - 273
EP  - 277
PB  - Wiley-Blackwell
CY  - Malden
ER  -