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 Citation (Scopus)

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

Fingerprint

Treponema pallidum
Carrier Proteins
Ligands
Glucose
Crystals
Proteins
Crystal structure
Topology
Spirochaetales
ATP-Binding Cassette Transporters
Syphilis

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

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title = "Crystal stuctures of MglB-2 (TP0684), a topologically variant d-glucose-binding protein from Treponema pallidum, reveal a ligand-induced conformational change",
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.",
keywords = "ABC transporter, Conformational change, Glucose-binding protein, Spirochete, Syphilis",
author = "Brautigam, {Chad A} and Deka, {Ranjit K.} and Liu, {Wei Z.} and Norgard, {Michael V}",
year = "2018",
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doi = "10.1002/pro.3373",
language = "English (US)",
journal = "Protein Science",
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T1 - Crystal stuctures of MglB-2 (TP0684), a topologically variant d-glucose-binding protein from Treponema pallidum, reveal a ligand-induced conformational change

AU - Brautigam, Chad A

AU - Deka, Ranjit K.

AU - Liu, Wei Z.

AU - Norgard, Michael V

PY - 2018/1/1

Y1 - 2018/1/1

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AB - 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.

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