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 |
Appears in Collections: | Articles |
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