Purification, crystallization and preliminary X-ray analysis of an aminoacylhistidine dipeptidase (PepD) from Vibrio alginolyticus

Chin-Yuan Chang, Yin Cheng Hsieh, Ting Yi Wang, Chun Jung Chen*, Tung-Kung Wu

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The aminoacylhistidine dipeptidase (PepD) protein encoded by Vibrio alginolyticus pepD was successfully overexpressed and characterized and the putative active-site residues responsible for metal binding and catalysis were identified. The purified enzyme contained two zinc ions per monomer. The recombinant dipeptidase enzyme, which was identified as a homodimer in solution, exhibited broad substrate specificity for Xaa-His dipeptides, with highest activity towards the His-His dipeptide. The purified protein was crystallized using the hanging-drop vapour-diffusion method. Preliminary crystallographic analysis showed that the crystal belonged to space group P61 or P65, with unit-cell parameters a = b = 80.42, c = 303.11 Å. The crystal contained two molecules per asymmetric unit and the predicted solvent content was 53.4%.

Original languageEnglish
Pages (from-to)216-218
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number3
DOIs
StatePublished - 13 Mar 2009

Keywords

  • Aminoacylhistidine dipeptidases
  • Metallopeptidases
  • Vibrio alginolyticus

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