| Crystal structure of zebrafish hatching enzyme 1 from the zebrafish Danio rerio. | |
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MedLine Citation:
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PMID: 20727360 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Fish hatching enzymes are zinc metalloproteases that digest the egg envelope (chorion) at the time of hatching. The crystal structure of zebrafish hatching enzyme 1 (ZHE1) has been solved at 1.10 Å resolution. ZHE1 is monomeric, is mitten shaped, and has a cleft at the center of the molecule. ZHE1 consists of three 3(10)-helices, three α-helices, and two β-sheets. The central cleft represents the active site of the enzyme that is crucial for substrate recognition and catalysis. Alanine-scanning mutagenesis of the two substrate peptides has shown that AspP1' contributes the most and that the residues at P4-P2' also contribute to the recognition of the major substrate peptide by ZHE1, whereas GluP3' and the hydrophobic residues at P4-P2, P2', and P5' contribute significantly to the recognition of the minor substrate peptide by ZHE1. Molecular models of these two substrate peptides bound to ZHE1 have been built based on the crystal structure of a transition-state analog inhibitor bound to astacin. In substrate-recognition models, the AspP1' in the major substrate peptide forms a salt bridge with Arg182 of ZHE1, while the GluP3' in the minor substrate peptide instead forms a salt bridge with Arg182. Thus, these two substrate peptides would be differently recognized by ZHE1. The shapes and electrostatic potentials of the substrate-binding clefts of ZHE1 and the structurally similar proteins astacin and bone morphogenetic protein 1 are significantly dissimilar due to different side chains, which would confer their distinctive substrate preferences. |
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Authors:
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Akitoshi Okada; Kaori Sano; Koji Nagata; Shigeki Yasumasu; Jun Ohtsuka; Akihiro Yamamura; Keiko Kubota; Ichiro Iuchi; Masaru Tanokura |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-08-18 |
Journal Detail:
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Title: Journal of molecular biology Volume: 402 ISSN: 1089-8638 ISO Abbreviation: J. Mol. Biol. Publication Date: 2010 Oct |
Date Detail:
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Created Date: 2010-10-04 Completed Date: 2010-10-19 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2985088R Medline TA: J Mol Biol Country: England |
Other Details:
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Languages: eng Pagination: 865-78 Citation Subset: IM |
Copyright Information:
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Copyright © 2010 Elsevier Ltd. All rights reserved. |
Affiliation:
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Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/3LQB |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Amino Acid Substitution Animals Catalytic Domain Crystallography, X-Ray Metalloendopeptidases / chemistry*, metabolism* Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Protein Conformation Protein Structure, Tertiary Sequence Alignment Zebrafish* |
| Chemical | |
Reg. No./Substance:
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EC 3.4.24.-/Metalloendopeptidases; EC 3.4.24.12/envelysin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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