The three-dimensional structure of aspergilloglutamic peptidase from Aspergillus niger

被引：14

作者：

Sasaki, H

Nakagawa, A

Muramatsu, T

Suganuma, M

Sawano, Y

Kojima, M

Kubota, K

Takahashi, K

Tanokura, M

机构：

[1] Univ Tokyo, Grad Sch Sci, Dept Biophys, Bunkyo Ku, Tokyo 1130033, Japan

[2] Tokiwa Jr Coll, Mito, Ibaraki 3108585, Japan

[3] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan

[4] Natl Canc Ctr, Res Inst, Div Biophys, Chuo Ku, Tokyo 1040045, Japan

[5] Univ Tokyo, Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo 1138657, Japan

[6] Tokyo Univ Pharm & Life Sci, Sch Life Sci, Hachioji, Tokyo 1920392, Japan

来源：

PROCEEDINGS OF THE JAPAN ACADEMY SERIES B-PHYSICAL AND BIOLOGICAL SCIENCES | 2004年 / 80卷 / 09期

关键词：

Aspergilloglutamic peptidase; catalytic residue; glutamic peptidase; three-dimensional structure; X-ray crystallography;

D O I：

10.2183/pjab.80.435

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Aspergilloglutamic peptidase from Aspergillus niger is a novel pepstatin-insensitive acid endopeptidase distinct from the well-studied aspartic peptidases, and thus is an interesting target for protein structure/function studies. In the present study, we have determined the three-dimensional structure of the enzyme by X-ray crystallography to a 1.4-Angstrom resolution. The results revealed that the enzyme has a unique structure, composed of two seven-stranded anti-parallel beta-sheets which form a beta-sandwich structure and appear to have a partial two-fold symmetry, suggesting its possible evolution by gene duplication and that the glutamic acid-110 and glutamine-24 in the heavy chain form a catalytic dyad, consistent with our results obtained by site-directed mutagenesis.

引用

页码：435 / 438

页数：4

共 17 条

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