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PDBsum entry 4z29

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protein Protein-protein interface(s) links
Signaling protein PDB id
4z29

 

 

 

 

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Contents
Protein chains
176 a.a.
Waters ×140
PDB id:
4z29
Name: Signaling protein
Title: Crystal structure of the magnetobacterial protein mtxa c-terminal domain
Structure: Magnetotaxis protein mtxa. Chain: a, b. Fragment: c-terminal domain, unp residues 25-313. Engineered: yes
Source: Magnetospirillum gryphiswaldense. Organism_taxid: 55518. Gene: mtxa, mgr_0208. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.03Å     R-factor:   0.187     R-free:   0.227
Authors: R.Zarivach,G.Davidov
Key ref: G.Davidov et al. (2015). Crystal structure of the magnetobacterial protein MtxA C-terminal domain reveals a new sequence-structure relationship. Front Mol Biosci, 2, 25. PubMed id: 26052516 DOI: 10.3389/fmolb.2015.00025
Date:
29-Mar-15     Release date:   03-Jun-15    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
A4TUL6  (A4TUL6_9PROT) -  Magnetotaxis protein MtxA from Magnetospirillum gryphiswaldense
Seq:
Struc:
313 a.a.
176 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.3389/fmolb.2015.00025 Front Mol Biosci 2:25 (2015)
PubMed id: 26052516  
 
 
Crystal structure of the magnetobacterial protein MtxA C-terminal domain reveals a new sequence-structure relationship.
G.Davidov, F.D.Müller, J.Baumgartner, R.Bitton, D.Faivre, D.Schüler, R.Zarivach.
 
  ABSTRACT  
 
Magnetotactic bacteria (MTB) are a diverse group of aquatic bacteria that have the magnetotaxis ability to align themselves along the geomagnetic field lines and to navigate to a microoxic zone at the bottom of chemically stratified natural water. This special navigation is the result of a unique linear assembly of a specialized organelle, the magnetosome, which contains a biomineralized magnetic nanocrystal enveloped by a cytoplasmic membrane. The Magnetospirillum gryphiswaldense MtxA protein (MGR_0208) was suggested to play a role in bacterial magnetotaxis due to its gene location in an operon together with putative signal transduction genes. Since no homology is found for MtxA, and to better understand the role and function of MtxA in MTBés magnetotaxis, we initiated structural and functional studies of MtxA via X-ray crystallography and deletion mutagenesis. Here, we present the crystal structure of the MtxA C-terminal domain and provide new insights into its sequence-structure relationship.
 

 

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