2013 Fiscal Year Final Research Report
Structure determination and Characterization of proline-specific aminopeptidases
Project/Area Number |
24790057
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Physical pharmacy
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Research Institution | Hyogo University of Health Sciences |
Principal Investigator |
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Project Period (FY) |
2012-04-01 – 2014-03-31
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Keywords | X線結晶解析 / X線溶液散乱 / 宇宙実験 / タンパク質 / コラーゲン / 基質認識 |
Research Abstract |
Proline-specific aminopeptidases are critical to the degradation of proline-rich peptides and proteins, such as collagen and its denatured form, gelatin. Collagens are the largest components in animal tissues and the most major hard-to-degrade proteins because of their unique fibrils composed of triple helical wound polypeptides. In this study, we crystallized three of the recombinant enzymes (Pz-A, Pz-B, and AM-1), and performed its preliminary X-ray crystallographic analysis. We have determined the entire structure of the these aminopeptidases, found a very unique apical domain sharing the interface with a domain containing a main active site and described about the characteristic structure and mechanism for the substrate recognition for proly peptides.
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[Journal Article] Crystallization and preliminary X-ray crystallographic analysis of Pz peptidase B from Geobacillus collagenovorans MO-12012
Author(s)
Nakano, H., Hosokawa, A., Tagawa, R., Inaka, K., Ohta, K., Nakatsu, T., Kato, H., Watanabe, K
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Journal Title
Acta Crystallographica
Volume: F68
Pages: 757-759
DOI
Peer Reviewed
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