Elucidation of Advanced Function by Combined High-Resolution Neutron and X-ray Analysis

• TAMADA Taro

  Quantum Beam Science Directorate, Japan Atomic Energy Agency

• KUROKI Ryota

  Quantum Beam Science Directorate, Japan Atomic Energy Agency

• KINOSHITA Takayoshi

  Graduate School of Science, Osaka Prefecture University

• TADA Toshiji

  Graduate School of Science, Osaka Prefecture University

Bibliographic Information

Other Title

• 中性子構造解析および超高分解能Ｘ線構造解析によるエラスターゼの高度な機能解明
• チュウセイシ コウゾウ カイセキ オヨビ チョウ コウ ブンカイノウ Xセン コウゾウ カイセキ ニ ヨル エラスターゼ ノ コウド ナ キノウ カイメイ

Abstract

To help resolve long-standing questions regarding the catalytic activity of the serine proteases the structure of porcine pancreatic elastase has been analyzed by high-resolution neutron (1.65 Å resolution) and X-ray (0.94 Å resolution) crystallography. In order to mimic the tetrahedral transition intermediate, a peptidic inhibitor was used. The neutron and X-ray data show that the hydrogen bond between His57 and Asp102 is not consistent with a low-barrier hydrogen which is predicted to have the hydrogen midway between the donor and acceptor atom. The neutron analysis also shows that the oxygen of the oxopropyl group of the inhibitor is present as an oxygen anion rather than a hydroxyl group, supporting the role of the “oxyanion hole” in stabilizing the tetrahedral intermediate in catalysis.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 52 (2), 133-138, 2010

  The Crystallographic Society of Japan

Details

• CRID: 1390282679063816704
• NII Article ID: 10026402487
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.52.133
• COI: 1:CAS:528:DC%2BC3cXntVGlsrs%3D
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 10691908
• Web Site: http://id.ndl.go.jp/bib/10691908
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I10691908
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed