Mechanistic Insight into the Function of the C-terminal PKD Domain of the Collagenolytic Serine Protease Deseasin MCP-01 from Deep Sea Pseudoalteromonas sp SM9913 BINDING OF THE PKD DOMAIN TO COLLAGEN RESULTS IN COLLAGEN SWELLING BUT DOES NOT UNWIND THE COLLAGEN TRIPLE HELIX

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	Mechanistic Insight into the Function of the C-terminal PKD Domain of the Collagenolytic Serine Protease Deseasin MCP-01 from Deep Sea Pseudoalteromonas sp SM9913 BINDING OF THE PKD DOMAIN TO COLLAGEN RESULTS IN COLLAGEN SWELLING BUT DOES NOT UNWIND THE COLLAGEN TRIPLE HELIX
	Wang, YK ; Zhao, GY ; Li, Y ; Chen, XL ; Xie, BB ; Su, HN ; Lv, YH ; He, HL ; Liu, H ; Hu, J ; Zhou, BC ; Zhang, YZ
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2010
卷号	285 期号:19 页码:7
ISSN号	0021-9258
通讯作者	Zhang, YZ (reprint author), Shandong Univ, Marine Biotechnol Res Ctr, State Key Lab Microbial Technol, Jinan 250100, Peoples R China
英文摘要	Deseasin MCP-01 is a bacterial collagenolytic serine protease. Its catalytic domain alone can degrade collagen, and its C-terminal PKD domain is a collagen-binding domain (CBD) that can improve the collagenolytic efficiency of the catalytic domain by an unknown mechanism. Here, scanning electron microscopy (SEM), atomic force microscopy (AFM), zeta potential, and circular dichroism spectroscopy were used to clarify the functional mechanism of the PKD domain in MCP-01 collagenolysis. The PKD domain observably swelled insoluble collagen. Its collagen-swelling ability and its improvement to the collagenolysis of the catalytic domain are both temperature-dependent. SEM observation showed the PKD domain swelled collagen fascicles with an increase of their diameter from 5.3 mu m to 8.8 mu m after 1 h of treatment, and the fibrils forming the fascicles were dispersed. AFM observation directly showed that the PKD domain bound collagen, swelled the microfibrils, and exposed the monomers. The PKD mutant W36A neither bound collagen nor disturbed its structure. Zeta potential results demonstrated that PKD treatment increased the net positive charges of the collagen surface. PKD treatment caused no change in the content or the thermostability of the collagen triple helix. Furthermore, the PKD-treated collagen could not be degraded by gelatinase. Therefore, though the triple helix monomers were exposed, the PKD domain could not unwind the collagen triple helix. Our study reveals the functional mechanism of the PKD domain of the collagenolytic serine protease MCP-01 in collagen degradation, which is distinct from that of the CBDs of mammalian matrix metalloproteases.
学科主题	Biochemistry & Molecular Biology
收录类别	SCI
语种	英语
WOS记录号	WOS:000277299700025
公开日期	2012-04-11
内容类型	期刊论文
源URL	[http://ir.sinap.ac.cn/handle/331007/6979]
专题	上海应用物理研究所_中科院上海应用物理研究所2004-2010年
推荐引用方式 GB/T 7714	Wang, YK,Zhao, GY,Li, Y,et al. Mechanistic Insight into the Function of the C-terminal PKD Domain of the Collagenolytic Serine Protease Deseasin MCP-01 from Deep Sea Pseudoalteromonas sp SM9913 BINDING OF THE PKD DOMAIN TO COLLAGEN RESULTS IN COLLAGEN SWELLING BUT DOES NOT UNWIND THE COLLAGEN TRIPLE HELIX[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2010,285(19):7.
APA	Wang, YK.,Zhao, GY.,Li, Y.,Chen, XL.,Xie, BB.,...&Zhang, YZ.(2010).Mechanistic Insight into the Function of the C-terminal PKD Domain of the Collagenolytic Serine Protease Deseasin MCP-01 from Deep Sea Pseudoalteromonas sp SM9913 BINDING OF THE PKD DOMAIN TO COLLAGEN RESULTS IN COLLAGEN SWELLING BUT DOES NOT UNWIND THE COLLAGEN TRIPLE HELIX.JOURNAL OF BIOLOGICAL CHEMISTRY,285(19),7.
MLA	Wang, YK,et al."Mechanistic Insight into the Function of the C-terminal PKD Domain of the Collagenolytic Serine Protease Deseasin MCP-01 from Deep Sea Pseudoalteromonas sp SM9913 BINDING OF THE PKD DOMAIN TO COLLAGEN RESULTS IN COLLAGEN SWELLING BUT DOES NOT UNWIND THE COLLAGEN TRIPLE HELIX".JOURNAL OF BIOLOGICAL CHEMISTRY 285.19(2010):7.