標題: Purification, crystallization and preliminary X-ray analysis of an aminoacylhistidine dipeptidase (PepD) from Vibrio alginolyticus
作者: Chang, Chin-Yuan
Hsieh, Yin-Cheng
Wang, Ting-Yi
Chen, Chun-Jung
Wu, Tung-Kung
生物科技學系
Department of Biological Science and Technology
公開日期: 1-Mar-2009
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 P6(1) or P6(5), with unit-cell parameters a = b = 80.42, c = 303.11 angstrom. The crystal contained two molecules per asymmetric unit and the predicted solvent content was 53.4%.
URI: http://dx.doi.org/10.1107/S174430910900092X
http://hdl.handle.net/11536/7524
ISSN: 1744-3091
DOI: 10.1107/S174430910900092X
期刊: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Volume: 65
Issue: 
起始頁: 216
結束頁: 218
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