Inter-phylum structural conservation of the magnetosome-associated TPR-containing protein, MamA

Natalie Zeytuni, Dror Baran, Geula Davidov, Raz Zarivach

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Magnetotactic bacteria enclose the magnetosome, a unique prokaryotic sub-cellular organelle that allows the biomineralization of magnetic nano-crystals. Membrane-coated magnetosomes are arranged into a linear chain that permits magnetotactic bacteria to navigate geomagnetic fields. Magnetosome assembly and biomineralization are controlled by conserved magnetosome-associated proteins, including MamA, a tetra-trico-peptide repeat (TPR)-containing protein that was shown to coat the magnetosome membrane. In this study, two MamA structures from Candidatus Magnetobacterium bavaricum (Mbav) were determined via X-ray crystallography. These structures confirm that Mbav MamA folds as a sequential TPR protein and shares a high degree of structural similarity with homologous MamA proteins from Magnetospirillum species. Furthermore, the two TPR-containing domains of MamA are separated by an interphylum-conserved region containing a flexible hinge that is involved in ligand binding and recognition. Finally, substantial differences were found in the local stabilization of the MamA N-terminal domain as a result of the loss of an evolutionary conserved salt bridge.

Original languageEnglish
Pages (from-to)479-487
Number of pages9
JournalJournal of Structural Biology
Volume180
Issue number3
DOIs
StatePublished - 1 Dec 2012

Keywords

  • Magnetosome
  • Magnetotactic bacteria
  • Protein-protein interactions
  • TPR proteins

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