Crystal Structure of a Major Outer Membrane Protein from Thermus thermophilus HB27

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Crystal structure of a major outer membrane protein from Thermus thermophilus HB27.

The thermophilic eubacterium Thermus thermophilus belongs to one of the oldest branches of evolution and has a multilayered cell envelope that differs from that of modern Gram-negative bacteria. Its outer membrane contains integral outer membrane proteins (OMPs), of which only a few are characterized. TtoA, a new beta-barrel OMP, was identified by searching the genome sequence of strain HB27 fo...

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Expression, crystallization and preliminary X-ray analysis of an outer membrane protein from Thermus thermophilus HB27.

The cell envelope of the thermophilic bacterium Thermus thermophilus is multilayered and includes an outer membrane with integral outer membrane proteins that are not well characterized. The hypothetical protein TTC0834 from T. thermophilus HB27 was identified as a 22 kDa outer membrane protein containing eight predicted beta-strands. TTC0834 was expressed with an N-terminal His tag in T. therm...

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Omp85(Tt) from Thermus thermophilus HB27: an ancestral type of the Omp85 protein family.

Proteins belonging to the Omp85 family are involved in the assembly of beta-barrel outer membrane proteins or in the translocation of proteins across the outer membrane in bacteria, mitochondria, and chloroplasts. The cell envelope of the thermophilic bacterium Thermus thermophilus HB27 is multilayered, including an outer membrane that is not well characterized. Neither the precise lipid compos...

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Expression, purification and characterization of recombinant protein tyrosine phosphatase from Thermus thermophilus HB27.

The low-molecular-weight protein tyrosine phosphatases (PTPase) exist ubiquitously in prokaryotes and eukaryotes and play important roles in the regulation of physiological activities. We report here the expression, purification and characterization of an active and soluble PTPase from Thermus thermophilus HB27 in Escherichia coli. This PTPase has an optimum pH range of 2.8-4.8 when using p-nit...

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Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8.

The TT1542 protein from Thermus thermophilus HB8 is annotated as a conserved hypothetical protein, and belongs to the DUF158 family in the Pfam database. A BLAST search revealed that homologs of TT1542 are present in a wide range of organisms. The TT1542 homologs in eukaryotes, PIG-L in mammals, and GPI12 in yeast and protozoa, have N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI) de-N-acet...

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ژورنال

عنوان ژورنال: Journal of Molecular Biology

سال: 2009

ISSN: 0022-2836

DOI: 10.1016/j.jmb.2008.12.003