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Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition

The Journal of Biological Chemistry

Aug 4, 2006

Kiyoshi ItoTadashi Yoshimoto

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Abstract

Aminopeptidase N from Escherichia coli is a broad specificity zinc exopeptidase belonging to aminopeptidase clan MA, family M1. The structures of the ligand-free form and the enzyme-bestatin complex were determined at 1.5- and 1.6-A resolution, respectively. The enzyme is composed of fo...read more

Mentioned in this Paper

Alkalescens-Dispar Group
Carboxy-Terminal Amino Acid
Tertiary Protein Structure
Protein Structure, Quaternary
Macromolecular Alteration
Aminooligopeptidase
Cytokinesis of the Fertilized Ovum
Crystallography, X-Ray
Aminopeptidase
Gastroschisis
Paper Details
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Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition

The Journal of Biological Chemistry

Aug 4, 2006

Kiyoshi ItoTadashi Yoshimoto

PMID: 16885166

DOI: 10.1074/jbc.m605203200

Abstract

Aminopeptidase N from Escherichia coli is a broad specificity zinc exopeptidase belonging to aminopeptidase clan MA, family M1. The structures of the ligand-free form and the enzyme-bestatin complex were determined at 1.5- and 1.6-A resolution, respectively. The enzyme is composed of fo...read more

Mentioned in this Paper

Alkalescens-Dispar Group
Carboxy-Terminal Amino Acid
Tertiary Protein Structure
Protein Structure, Quaternary
Macromolecular Alteration
Aminooligopeptidase
Cytokinesis of the Fertilized Ovum
Crystallography, X-Ray
Aminopeptidase
Gastroschisis

Feeds With Similar Papers

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.

Related Papers

Proceedings of the National Academy of Sciences of the United States of America

Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site(opens in new tab)

Proceedings of the National Academy of Sciences of the United States of AmericaAugust 30, 2006
Anthony AddlagattaBrian W Matthews
Paper Details
References
  • References
  • Citations50
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations50
12345

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