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

@article{citeulike:3822483, abstract = {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 for the presence of a C-terminal signature sequence. The structure of TtoA was determined to a resolution of 2.8 A, representing the first crystal structure of an OMP from a thermophilic bacterium. TtoA consists of an eight-stranded beta-barrel with a large extracellular part to which a divalent cation is bound. A five-stranded extracellular beta-sheet protrudes out of the membrane-embedded transmembrane barrel and is stabilized by a disulfide bridge. The edge of this beta-sheet forms crystal contacts that could mimic interactions with other proteins. In modern Gram-negative bacteria, the C-terminal signature sequence of OMPs is required for binding to an Omp85 family protein as a prerequisite for its assembly. We present hints that a similar assembly pathway exists in T. thermophilus by an in vitro binding assay, where unfolded TtoA binds to the Thermus Omp85 family protein TtOmp85, while a mutant without the signature sequence does not.}, author = {Brosig, Alexander and Nesper, Jutta and Boos, Winfried and Welte, Wolfram and Diederichs, Kay}, citeulike-article-id = {3822483}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.jmb.2008.12.003}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19101566}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19101566}, day = {10}, doi = {10.1016/j.jmb.2008.12.003}, issn = {1089-8638}, journal = {Journal of molecular biology}, keywords = {bacteria, beta\_barrel, crystallography, folding, membrane, protein, structure, thermophile}, month = {December}, posted-at = {2008-12-24 00:14:06}, priority = {3}, title = {Crystal Structure of a Major Outer Membrane Protein from Thermus thermophilus HB27.}, url = {http://dx.doi.org/10.1016/j.jmb.2008.12.003}, year = {2008} }

TY - JOUR ID - citeulike:3822483 L3 - citeulike-article-id:3822483 N2 - 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 for the presence of a C-terminal signature sequence. The structure of TtoA was determined to a resolution of 2.8 A, representing the first crystal structure of an OMP from a thermophilic bacterium. TtoA consists of an eight-stranded beta-barrel with a large extracellular part to which a divalent cation is bound. A five-stranded extracellular beta-sheet protrudes out of the membrane-embedded transmembrane barrel and is stabilized by a disulfide bridge. The edge of this beta-sheet forms crystal contacts that could mimic interactions with other proteins. In modern Gram-negative bacteria, the C-terminal signature sequence of OMPs is required for binding to an Omp85 family protein as a prerequisite for its assembly. We present hints that a similar assembly pathway exists in T. thermophilus by an in vitro binding assay, where unfolded TtoA binds to the Thermus Omp85 family protein TtOmp85, while a mutant without the signature sequence does not. JF - Journal of molecular biology SN - 1089-8638 TI - Crystal Structure of a Major Outer Membrane Protein from Thermus thermophilus HB27. KW - bacteria KW - beta_barrel KW - crystallography KW - folding KW - membrane KW - protein KW - structure KW - thermophile AU - Brosig, Alexander AU - Nesper, Jutta AU - Boos, Winfried AU - Welte, Wolfram AU - Diederichs, Kay PY - 2008/12/10/ UR - http://dx.doi.org/10.1016/j.jmb.2008.12.003 ER -