Unknown

Dataset Information

0

Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC.


ABSTRACT: 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 I2. 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.

SUBMITTER: Wilding M 

PROVIDER: S-EPMC5287375 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC.

Wilding Matthew M   Scott Colin C   Newman Janet J   Peat Thomas S TS  

Acta crystallographica. Section F, Structural biology communications 20170101 Pt 1


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 I2. The crystals diffracted X-rays to 2.07 Å resolution and data were c  ...[more]

Similar Datasets

| S-EPMC5287376 | biostudies-literature
| S-EPMC4854569 | biostudies-literature
| S-EPMC4907197 | biostudies-literature
| S-EPMC5426288 | biostudies-literature
| S-EPMC6450518 | biostudies-literature
| PRJNA248604 | ENA
| PRJNA248598 | ENA
| S-EPMC5287369 | biostudies-literature
| S-EPMC4244111 | biostudies-literature
| S-EPMC6715241 | biostudies-literature