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PMID: 7298619 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

The three-dimensional structure of the lysozyme produced by Streptomyces erythraeus.

The Journal of biological chemistry ·Vol. 256 ·No. 22 ·1981-11-25 ·Pages 11600-2

Harada S, Sarma R, Kakudo M, Hara S, Ikenaka T

Abstract

Streptomyces erythraeus lysozyme is different in its amino acid composition, primary structure, and specificity from all other mammalian lysozymes. The structure of the crystalline enzyme has been determined by x-ray diffraction analysis to a resolution of 2.9 A using multiple isomorphous replacement. The primary structure of the enzyme is only partially known and therefore the electron density map has been fitted with all the atoms of the main polypeptide chain and some atoms of the side chain. The enzyme consists of three different domains, and about 18% of the structure has helical conformation. A comparison of the tertiary structure of the bacterial lysozyme with either the mammalian or phage lysozyme does not show any obvious similarities.

MeSH Terms
Amino Acids/analysis Models, Molecular Muramidase/metabolism Protein Conformation Species Specificity Streptomyces/enzymology Substrate Specificity X-Ray Diffraction
Chemicals
Amino Acids Muramidase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Harada S
Sarma R
Kakudo M
Hara S
Ikenaka T
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1981-11-25
Pages
11600-2
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NCI NIH HHS · CA25048 · United States
NIGMS NIH HHS · GM25883 · United States
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