PDBsum entry 3ml0

Hydrolase

PDB id: 3ml0

Contents

Protein chains

195 a.a. *

551 a.a. *

Metals

_CA

* Residue conservation analysis

PDB id:

3ml0

Name:

Hydrolase

Title:

Thermostable penicillin g acylase from alcaligenes faecalis in tetragonal form

Structure:

Penicillin g acylase, alpha subunit. Chain: a. Synonym: penicillin g amidase. Engineered: yes. Penicillin g acylase, beta subunit. Chain: b. Synonym: penicillin g amidase. Engineered: yes

Source:

Alcaligenes faecalis. Organism_taxid: 511. Gene: pac. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.50Å R-factor: 0.269 R-free: 0.283

Authors:

N.K.Varshney,R.S.Kumar,Z.Ignatova,E.Dodson,C.G.Suresh

Key ref:

N.K.Varshney et al. (2012). Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis. Acta Crystallogr Sect F Struct Biol Cryst Commun, 68, 273-277. PubMed id: 22442220 DOI: 10.1107/S1744309111053930

Date:

16-Apr-10 Release date: 05-May-10

Protein chain

O34142  (O34142_ALCFA) -  Penicillin G acylase from Alcaligenes faecalis

Seq: 816 a.a.

Struc: 195 a.a.

Protein chain

O34142  (O34142_ALCFA) -  Penicillin G acylase from Alcaligenes faecalis

Seq: 816 a.a.

Struc: 551 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.3.5.1.11 - penicillin amidase.
• Pathway: Penicillin Biosynthesis and Metabolism
• Reaction: a penicillin + H2O = 6-aminopenicillanate + a carboxylate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S1744309111053930

Acta Crystallogr Sect F Struct Biol Cryst Commun 68:273-277 (2012)

PubMed id: 22442220

Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis.

N.K.Varshney, R.S.Kumar, Z.Ignatova, A.Prabhune, A.Pundle, E.Dodson, C.G.Suresh.

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.