Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP

Sahil Balotra; Janet Newman; Nigel G French; Lyndall J Briggs; Thomas S Peat; Colin Scott

doi:10.1107/S2053230X13034705

Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP

Acta Crystallogr F Struct Biol Commun. 2014 Mar;70(Pt 3):310-5. doi: 10.1107/S2053230X13034705. Epub 2014 Feb 19.

Authors

Sahil Balotra¹, Janet Newman², Nigel G French¹, Lyndall J Briggs¹, Thomas S Peat², Colin Scott¹

Affiliations

¹ Ecosystem Sciences, CSIRO, GPO Box 1700, Canberra, ACT 2601, Australia.
² Materials, Science and Engineering, CSIRO, 343 Royal Parade, Parkville, VIC 3052, Australia.

Abstract

The allophanate hydrolase from Pseudomonas sp. strain ADP was expressed and purified, and a tryptic digest fragment was subsequently identified, expressed and purified. This 50 kDa construct retained amidase activity and was crystallized. The crystals diffracted to 2.5 Å resolution and adopted space group P21, with unit-cell parameters a = 82.4, b = 179.2, c = 112.6 Å, β = 106.6°.

Keywords: AtzF; Pseudomonas sp. strain ADP; allphanate hydrolase; amidase domain.

MeSH terms

Allophanate Hydrolase / chemistry*
Amidohydrolases / chemistry
Bacterial Proteins / chemistry*
Crystallization
Crystallography, X-Ray
Enzyme Stability
Proteolysis
Pseudomonas / enzymology*
Sequence Analysis, Protein
Trypsin / chemistry

Substances

Bacterial Proteins
Trypsin
Amidohydrolases
amidase
Allophanate Hydrolase