3VTX

Crystal structure of MamA protein

Summary for 3VTX

• Entry DOI: 10.2210/pdb3vtx/pdb
• Related: 3VTY
• Descriptor: MamA, GLYCEROL (3 entities in total)
• Functional Keywords: tetratricopeptide repeats (tpr) containing protein, peptide binding protein, protein binding
• Biological source: Candidatus Magnetobacterium bavaricum
• Total number of polymer chains: 2
• Total formula weight: 41481.73

Authors

Zeytuni, N.,Baran, D.,Davidov, G.,Zarivach, R. (deposition date: 2012-06-08, release date: 2012-10-31, Last modification date: 2024-03-20)

Primary citation

Zeytuni, N.,Baran, D.,Davidov, G.,Zarivach, R.
Inter-phylum structural conservation of the magnetosome-associated TPR-containing protein, MamA
J.Struct.Biol., 180:479-487, 2012

PubMed 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.

PubMed: 22917855
DOI: 10.1016/j.jsb.2012.08.001

Experimental method

X-RAY DIFFRACTION (1.75 Å)