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The Three Dimensional Structure of the Lysozyme from Bacteriophage T4

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Matthews, B. W., Remington, S. J.·1974·Proceedings of the National Academy of Sciences

Abstract

The three dimensional structure of the lysozyme from bacteriophage T4 has been determined from a 2.5 Å resolution electron density map. About 60% of the molecule is in a helical conformation and there is one region consisting of antiparallel β-structure. The polypeptide backbone folds into two distinct lobes linked in part by a long helix. In the region between the two lobes, there is a cleft which deepens into a hole or cavity, about 6-8 Å in diameter, extending from one side of the molecule to the other. This opening is closed off by side chains which extend to within 3-5 Å of each other. A number of mutant lysozymes in which residues in the vicinity of the opening are modified have markedly reduced catalytic activity, suggesting that this region of the molecule may be catalytically important. The three dimensional structure of T4 phage lysozyme is quite different from that of hen egg-white lysozyme although it is not clear at this time whether or not the mechanisms of catalysis of the respective enzymes are related.

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Metadata

Authors
Matthews, B. W., & Remington, S. J.
Venue
Proceedings of the National Academy of Sciences
Published
1974-10
Volume
71
Issue
10
Pages
4178-4182
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2018529040
Cited by
176
References
1
FWCI
5.05
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The Three Dimensional Structure of the Lysozyme from Bacteriophage T4. https://app.cochat.ai/papers/10.1073/pnas.71.10.4178
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Matthews, B. W., & Remington, S. J. (1974). The Three Dimensional Structure of the Lysozyme from Bacteriophage T4. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.71.10.4178

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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