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Article

Structure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile3-->Pro.

Journal of molecular biology - 5 Oct 1992

Dixon M M, Nicholson H, Shewchuk L, Baase W A, Matthews B W

Abstract excerpt

The mutant T4 phage lysozyme in which isoleucine 3 is replaced by proline (I3P) crystallizes in an orthorhombic form with two independent molecules in the asymmetric unit. Relative to wild-type lysozyme, which crystallizes in a trigonal form, the two I3P molecules undergo large hinge-bending displacements with the alignments of the amino-terminal and carboxy-terminal domains changed by 28.9 degrees and 32.9...

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Identifiers

PMID: 1404394
DOI: 10.1016/0022-2836(92)90231-8

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile3-->Pro.PMID 1404394Read ↗

A mutant T4 lysozyme displays five different crystal conformations.Semantic proximity Read ↗

Lessons from the lysozyme of phage T4.Semantic proximity Read ↗

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The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme.Semantic proximity Read ↗

A remote prolyl isomerization controls domain assembly via a hydrogen bonding network.Semantic proximity Read ↗

Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.Semantic proximity Read ↗

Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein.Semantic proximity Read ↗

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