Thermotoga maritima

It can ferment peptides, but not as the sole carbon source [223]. Hydrogen (or hydrogen sulfide), acetate, and CO2 are the primary fermentation products [224]. In addition to its fermentative metabolism, T. maritima may also respire by using Fe(III) [225], elemental sulfur [226], and thiosulfate as electron acceptors. 

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Brazzolotto X, JK Rubach, J Gaillard, S Gambrelli, M Atta, M Fontecave (2006) The [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster. J Biol Chem 279, 281 769-774. 

Juszczak A, S Aono, MWW Adams (1991) The extremely thermophilic eubacterium Thermotoga maritima, contains a novel iron-hydrogenase whose cellular activity is dependent upon tungsten. J Biol Chem 266 13834-13841. 

Toms AV, C Kinsland, DE McCloskey, AE Pegg, SE Ealick (2004) Evolutiouary liuks as revealed hy the structure of Thermotoga maritima 5-adenosylmethionine decarboxylase. J Biol Chem 279 33837-33846. 

Nelson, K. E., Clayton, R. A., Gill, S. R., Gwinn, M. L. et al. (1999), Evidence for lateral gene transfer between archaea and bacteria from genome sequence of Thermotoga maritima , Nature (London), 399, 323-329. 

F. Alberto, E. Jordi, B. Henrissat, and M. Czjzek, Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose, Biochem. J., 395 (2006) 4574-62. 

Fig. 6. Distribution of the most common folds in selected bacterial, archaeal, and eukaryotic proteomes. The vertical axis shows the fraction of all predicted folds in the respective proteome. Fold name abbreviations FAD/NAD, FAD/NAD(P)-binding Rossman-like domains TIM, TIM-barrel domains SAM-MTR, S-adenosylmethionine-dependent methyltransferases PK, serine-threonine protein kinases PP-Loop, ATP pyrophosphatases. mge, Mycoplasma genitalium rpr, Rickettsiaprowazekii hh x, Borrelia burgdorferi ctr, Chlamydia trachomatis hpy, Helicobacter pylori tma, Thermotoga maritima ssp, Synechocystis sp. mtu, Mycobacterium tuberculosis eco, Escherichia coli mja, Methanococcus jannaschii pho, Pyrococcus horikoshii see, Saccharomyces cerevisiae, cel, Caenorhabditis elegans.

Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature 399, 323—329. 

Zaiss, K. and R. Jaenicke. 1999. Thermodynamic study of phosphoglycerate kinase from Thermotoga maritima and its isolated domains reversible thermal unfolding monitored by differential scanning calorimetry and circular dichroism spectroscopy. Biochemistry 38 4633 -639. 

Dihydrofolate reductase from Thermotoga maritima hydride transfer from NADPH to 7,8-DHE... 

Song, H., Bochtlee, M., Azim, M., Hartmann, C., Huber, R., and Ramachandean, R. Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV. Biophys Chem. 2003, 100, 437-452. 

Kaiser IT, Clausen T, Bourenkow GP, et al. 2000. Crystal structure of a NifS-like protein from Thermotoga maritima Implications for iron-snlfur clnster assembly. J Mol Biol 297 451-64. 

Fig. 4. Stereoviews of TmCsp. (A) Stereoview of a superposition of the backbone atoms of the 21 accepted structures of TmCsp. (B) Stereoview of a representative ribbon diagram of TmCsp. The secondary-structure elements are indicated. (C) Stereoview of the solution NMR structure of TmCsp (rotated ribbon diagram). Location of a possible peripheral ion cluster. Reprinted from Eur. J. Biochem., Vol. 268, W. Kremer, B. Schuler, S. Harrieder, M. Geyer, W. Gronwald, C. Welker, R. Jaenicke and H. R. Kalbitzer, Solution NMR structure of the cold-shock protein from the hyperthermo-philic bacterium Thermotoga maritima , pp. 2527-2539, Copyright 2001, with permission from Blackwell Science.

The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. A structural proteomic project used the sequenced genome of the thermophilic Methanobacterium thermoautotrophicum as a source of targets for structure determination.As expected, proteins from M. thermoautotrophicum possess high thermostability with a transition midpoint temperature between 68 and 98 °C. Small proteins were C- and N-labelled and their solution structures were solved using multinuclear and multidimensional NMR spectro-scopy. The project was also extended to some proteins from Thermotoga maritima ... 

Figure 2.4 Structures of histone deacetylases from the sirtuin family. Ribbon representation of the structures of the conserved catalytic domain of histone deacetylases (a) Homo sapiens SirT2 (PDB code IjSf) and (b) Thermotoga maritima Sir2 bound to NAD and an acetylated p53 peptide (PDB code 2h4f).

Lesley, S. A., Kuhn, P, Godzik, A., Deacon, A. M., Mathews, I., Kreusch, A., et al. (2002). Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline. Proc. Natl. Acad. Sci. USA 99,11664-11669. 

Fig. 6. Superposition of ligands 1-deoxynojirimycin 2 (yellow, PDB 2J77) and castanospermine 8 (green, PDB 2CBU) bound to Thermotoga maritima p-glucosidase. The ring nitrogen atoms, all hydroxyl groups in the pyranoid rings, as well as 0-1 (8) and the primary 0-6 (2), respectively, are closely matched.

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