 |
PDBsum entry 3ml0
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Crystallization and X-Ray structure analysis of a thermostable penicillin g acylase from alcaligenes faecalis.
|
|
|
Authors
|
|
N.K.Varshney,
R.S.Kumar,
Z.Ignatova,
A.Prabhune,
A.Pundle,
E.Dodson,
C.G.Suresh.
|
|
|
Ref.
|
|
Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012,
68,
273-277.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
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: C222(1), with unit-cell parameters a = 72.9, b = 86.0, c = 260.2 ,
and P4(1)2(1)2, with unit-cell parameters a = b = 85.6, c = 298.8 . Data were
collected at 293 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
β-chain. A disulfide bridge has been identified in the structure that was not
found in the other two known penicillin G cylase structures. The presence of the
disulfide bridge is perceived to be one factor that confers higher stability to
this enzyme.
|
|
|
|
|
|
|
