Crystal stuctures of MglB-2 (TP0684), a topologically variant d-glucose-binding protein from Treponema pallidum, reveal a ligand-induced conformational change

Chad A Brautigam, Ranjit K. Deka, Wei Z. Liu, Michael V Norgard

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

Previously, we determined the crystal structure of apo-TpMglB-2, a d-glucose-binding component of a putative ABC transporter from the syphilis spirochete Treponema pallidum. The protein had an unusual topology for this class of proteins, raising the question of whether the d-glucose-binding mode would be different in TpMglB-2. Here, we present the crystal structures of a variant of TpMglB-2 with and without d-glucose bound. The structures demonstrate that, despite its aberrant topology, the protein undergoes conformational changes and binds d-glucose similarly to other Mgl-type proteins, likely facilitating d-glucose uptake in T. pallidum.

Original languageEnglish (US)
JournalProtein Science
DOIs
StateAccepted/In press - Jan 1 2018

Keywords

  • ABC transporter
  • Conformational change
  • Glucose-binding protein
  • Spirochete
  • Syphilis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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