Similar structures to the E-to-H helix unit in the globin-like fold are found in other helical folds

Masanari Matsuoka, Aoi Fujita, Yosuke Kawai, Takeshi Kikuchi

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

A protein in the globin-like fold contains six alpha-helices, A, B, E, F, G and H. Among them, the E-to-H helix unit (E, F, G and H helices) forms a compact structure. In this study, we searched similar structures to the E-to-H helix of leghomoglobin in the whole protein structure space using the Dali program. Several similar structures were found in other helical folds, such as KaiA/RbsU domain and Type III secretion system domain. These observations suggest that the E-to-H helix unit may be a common subunit in the whole protein 3D structure space. In addition, the common conserved hydrophobic residues were found among the similar structures to the E-to-H helix unit. Hydrophobic interactions between the conserved residues may stabilize the 3D structures of the unit. We also predicted the possible compact regions of the units using the average distance method.

Original languageEnglish
Pages (from-to)268-288
Number of pages21
JournalBiomolecules
Volume4
Issue number1
DOIs
Publication statusPublished - 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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