Solution structure and dynamics of C-terminal regulatory domain of Vibrio vulnificus extracellular metalloprotease |
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Authors: | Ji-Hye Yun Heeyoun Kim Jung Eun Park Jung Sup Lee Weontae Lee |
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Affiliation: | 1. Department of Food Science and Nutrition, College of Health, Welfare and Education, Gwangju University, Gwangju 503-703, Republic of Korea;2. Department of Pharmaceutical Engineering, Institute of Biomolecule Reconstruction, Sun Moon University, Asansi, Chungnam 336-708, Republic of Korea;3. Department of Biotechnology, The Catholic University of Korea, Bucheon, Gyeonggi-do 420-743, Republic of Korea;1. Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 120–749, Korea;2. Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120–749, Korea |
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Abstract: | An extracellular metalloprotease (vEP) secreted by Vibrio vulnificus ATCC29307 is a 45-kDa proteolytic enzyme that has prothrombin activation and fibrinolytic activities during bacterial infection. The action of vEP could result in clotting that could serve to protect the bacteria from the host defense machinery. Very recently, we showed that the C-terminal propeptide (C-ter100), which is unique to vEP, is involved in regulation of vEP activity. To understand the structural basis of this function of vEP C-ter100, we have determined the solution structure and backbone dynamics using multidimensional nuclear magnetic resonance spectroscopy. The solution structure shows that vEP C-ter100 is composed of eight anti-parallel β-strands with a unique fold that has a compact β-barrel formation which stabilized by hydrophobic and hydrogen bonding networks. Protein dynamics shows that the overall structure, including loops, is very rigid and stabilized. By structural database analysis, we found that vEP C-ter100 shares its topology with that of the collagen-binding domain of collagenase, despite low sequence homology between the two domains. Fluorescence assay reveals that vEP C-ter100 interacts strongly with iron (Fe3+). These findings suggest that vEP protease might recruit substrate molecules, such as collagen, by binding at C-ter100 and that vEP participates in iron uptake from iron-withholding proteins of the host cell during infection. |
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