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Bioinformatic analysis of the TonB protein family

Chu, Byron C. H ; Peacock, R. Sean ; Vogel, Hans J

Biometals, 2007-06, Vol.20 (3-4), p.467-483, Article 467 [Periódico revisado por pares]

Netherlands: New York : Kluwer Academic Publishers-Plenum Publishers

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Título:
Bioinformatic analysis of the TonB protein family
Autor: Chu, Byron C. H ; Peacock, R. Sean ; Vogel, Hans J
Assuntos: Amino Acid Sequence ; Amino acids ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - classification ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bioinformatics ; Clusters ; Computational Biology ; Conserved sequence ; Coordination compounds ; Domains ; E coli ; Energy transduction ; Escherichia coli ; Gram-negative bacteria ; Helices ; Homology ; Iron ; Iron transport ; Membrane Proteins - chemistry ; Membrane Proteins - classification ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Molecular Sequence Data ; Multiple sequence alignment ; Phylogeny ; Protein Conformation ; Protein structure ; Proteins ; Secondary structure ; Sequence Alignment ; Sequence Analysis, Protein ; Structure-function relationships ; TonB ; TonB protein ; Variable region ; Vitamin B12
É parte de: Biometals, 2007-06, Vol.20 (3-4), p.467-483, Article 467
Notas: http://dx.doi.org/10.1007/s10534-006-9049-4
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Descrição: TonB is a protein prevalent in a large number of Gram-negative bacteria that is believed to be responsible for the energy transduction component in the import of ferric iron complexes and vitamin B₁₂ across the outer membrane. We have analyzed all the TonB proteins that are currently contained in the Entrez database and have identified nine different clusters based on its conserved 90-residue C-terminal domain amino acid sequence. The vast majority of the proteins contained a single predicted cytoplasmic transmembrane domain; however, nine of the TonB proteins encompass a ~290 amino acid N-terminal extension homologous to the MecR1 protein, which is composed of three additional predicted transmembrane helices. The periplasmic linker region, which is located between the N-terminal domain and the C-terminal domain, is extremely variable both in length (22-283 amino acids) and in proline content, indicating that a Pro-rich domain is not a required feature for all TonB proteins. The secondary structure of the C-terminal domain is found to be well preserved across all families, with the most variable region being between the second α-helix and the third β-strand of the antiparallel β-sheet. The fourth β-strand found in the solution structure of the Escherichia coli TonB C-terminal domain is not a well conserved feature in TonB proteins in most of the clusters. Interestingly, several of the TonB proteins contained two C-terminal domains in series. This analysis provides a framework for future structure-function studies of TonB, and it draws attention to the unusual features of several TonB proteins.
Editor: Netherlands: New York : Kluwer Academic Publishers-Plenum Publishers
Idioma: Inglês;Holandês

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Bioinformatic analysis of the TonB protein family

Chu, Byron C. H ; Peacock, R. Sean ; Vogel, Hans J

Netherlands: New York : Kluwer Academic Publishers-Plenum Publishers

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