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

*此作品的通信作者

研究成果: Article同行評審

3 引文 斯高帕斯(Scopus)

摘要

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%.

原文English
頁(從 - 到)216-218
頁數3
期刊Acta Crystallographica Section F: Structural Biology and Crystallization Communications
65
發行號3
DOIs
出版狀態Published - 13 3月 2009

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