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Article

Proteolysis of truncated hemolysin A yields a stable dimerization interface.

Acta crystallographica. Section F, Structural biology communications - 1 Mar 2017

Novak Walter R P, Bhattacharyya Basudeb, Grilley Daniel P, Weaver Todd M

Abstract excerpt

Wild-type and variant forms of HpmA265 (truncated hemolysin A) from Proteus mirabilis reveal a right-handed, parallel β-helix capped and flanked by segments of antiparallel β-strands. The low-salt crystal structures form a dimeric structure via the implementation of on-edge main-chain hydrogen bonds donated by residues 243-263 of adjacent monomers. Surprisingly, in the high-salt structures of two variants, Y134A...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 28291749
DOI: 10.1107/S2053230X17002102
PMCID: PMC5349307

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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