Crystallization and preliminary X-ray analysis of recombinant Glomerella cingulata cutinase

Mun Peak Nyon, David W. Rice, John M. Berrisford, Huazhang Huang, Arthur J G Moir, C. Jeremy Craven, Sheila Nathan, Nor Muhammad Mahadi, Farah Diba Abu Bakar

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Cutinase catalyzes the hydrolysis of water-soluble esters and long-chain triglycerides and belongs to the family of serine hydrolases. The enzyme is thought to represent an evolutionary link between the esterase and lipase families and has potential applications in a wide range of industrial hydrolytic processes, for which an understanding of the molecular basis of its substrate specificity is critical. Glomerella cingulata cutinase has been cloned and the protein has been overexpressed in Escherichia coli, purified and subsequently crystallized in a wide range of different crystal forms in the presence and absence of inhibitors. The best crystals are those of the apo cutinase, which diffract to beyond 1.6 Å resolution and belong to space group P4 1212 or P43212. Crystals of cutinase with the inhibitors PETFP or E600 belong to space groups P212 121 and P21, respectively, and diffract to approximately 2.5 Å resolution. All of the crystals are suitable for structural studies, which are currently ongoing.

Original languageEnglish
Pages (from-to)504-508
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number6
DOIs
Publication statusPublished - 2008

Fingerprint

Phyllachorales
X ray analysis
Crystallization
X-Rays
crystallization
Crystals
inhibitors
crystals
x rays
Hydrolases
Esterases
Substrate Specificity
Escherichia
Lipase
Serine
Escherichia coli
hydrolysis
enzymes
esters
Hydrolysis

Keywords

  • Cutinase
  • Glomerella cingulata
  • Inhibitor complexes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics
  • Medicine(all)

Cite this

Crystallization and preliminary X-ray analysis of recombinant Glomerella cingulata cutinase. / Nyon, Mun Peak; Rice, David W.; Berrisford, John M.; Huang, Huazhang; Moir, Arthur J G; Craven, C. Jeremy; Nathan, Sheila; Mahadi, Nor Muhammad; Abu Bakar, Farah Diba.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 64, No. 6, 2008, p. 504-508.

Research output: Contribution to journalArticle

Nyon, Mun Peak ; Rice, David W. ; Berrisford, John M. ; Huang, Huazhang ; Moir, Arthur J G ; Craven, C. Jeremy ; Nathan, Sheila ; Mahadi, Nor Muhammad ; Abu Bakar, Farah Diba. / Crystallization and preliminary X-ray analysis of recombinant Glomerella cingulata cutinase. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2008 ; Vol. 64, No. 6. pp. 504-508.
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