Premium
Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC
Author(s) -
Wilding Matthew,
Scott Colin,
Newman Janet,
Peat Thomas S.
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16019658
Subject(s) - transamination , heterologous expression , putrescine , beamline , strain (injury) , protein data bank (rcsb pdb) , chemistry , molecular replacement , crystallization , crystallography , enzyme , crystal structure , stereochemistry , biochemistry , biology , recombinant dna , physics , optics , organic chemistry , gene , beam (structure) , anatomy
The putrescine aminotransferase KES24511 from Pseudomonas sp. strain AAC was previously identified as an industrially relevant enzyme based on the discovery that it is able to promiscuously catalyse the transamination of 12‐aminododecanoic acid. Here, the cloning, heterologous expression, purification and successful crystallization of the KES24511 protein are reported, which ultimately generated crystals adopting space group I 2. The crystals diffracted X‐rays to 2.07 Å resolution and data were collected using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4a6t as the search model.