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PDBsum entry 3vtx

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protein ligands Protein-protein interface(s) links
Protein binding PDB id
3vtx

 

 

 

 

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Contents
Protein chains
181 a.a.
Ligands
GOL ×2
Waters ×376
PDB id:
3vtx
Name: Protein binding
Title: Crystal structure of mama protein
Structure: Mama. Chain: a, b. Engineered: yes
Source: Candidatus magnetobacterium bavaricum. Organism_taxid: 29290. Strain: mbav. Gene: mama. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.75Å     R-factor:   0.164     R-free:   0.200
Authors: N.Zeytuni,D.Baran,G.Davidov,R.Zarivach
Key ref: N.Zeytuni et al. (2012). Inter-phylum structural conservation of the magnetosome-associated TPR-containing protein, MamA. J Struct Biol, 180, 479-487. PubMed id: 22917855
Date:
08-Jun-12     Release date:   31-Oct-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
K7N5L8  (K7N5L8_9BACT) -  MamA from Candidatus Magnetobacterium bavaricum
Seq:
Struc:
184 a.a.
181 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
J Struct Biol 180:479-487 (2012)
PubMed id: 22917855  
 
 
Inter-phylum structural conservation of the magnetosome-associated TPR-containing protein, MamA.
N.Zeytuni, D.Baran, G.Davidov, R.Zarivach.
 
  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.
 

 

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