New crystal forms of the integral membrane Escherichia coli quinol:fumarate reductase suggest that ligands control domain movement

C. A. Starbird, Thomas M. Tomasiak, Prashant K. Singh, Victoria Yankovskaya, Elena Maklashina, Michael Eisenbach, Gary Cecchini, T. M. Iverson

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Quinol:fumarate reductase (QFR) is an integral membrane protein and a member of the respiratory Complex II superfamily. Although the structure of Escherichia coli QFR was first reported almost twenty years ago, many open questions of catalysis remain. Here we report two new crystal forms of QFR, one grown from the lipidic cubic phase and one grown from dodecyl maltoside micelles. QFR crystals grown from the lipid cubic phase processed as P1, merged to 7.5 Å resolution, and exhibited crystal packing similar to previous crystal forms. Crystals grown from dodecyl maltoside micelles processed as P21, merged to 3.35 Å resolution, and displayed a unique crystal packing. This latter crystal form provides the first view of the E. coli QFR active site without a dicarboxylate ligand. Instead, an unidentified anion binds at a shifted position. In one of the molecules in the asymmetric unit, this is accompanied by rotation of the capping domain of the catalytic subunit. In the other molecule, this is associated with loss of interpretable electron density for this same capping domain. Analysis of the structure suggests that the ligand adjusts the position of the capping domain.

Original languageEnglish (US)
Pages (from-to)100-104
Number of pages5
JournalJournal of Structural Biology
Volume202
Issue number1
DOIs
StatePublished - Apr 2018

Keywords

  • Catalysis
  • Complex II
  • Conformational Change
  • Crystallography
  • Fumarate reductase
  • Lipid cubic phase
  • Membrane protein
  • Protein-protein interaction
  • Respiratory chain

ASJC Scopus subject areas

  • Structural Biology

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