Aquifex aeolicus

Fig. 8. Principal component analysis of the distribution of the predicted folds in bacterial, archaeal, and eukaryotic proteomes. (a) First and second principal components (b) third and fourth principal components. Aae, Aquifex aeolicus Mge, Mycoplasm genitalium Mpn, Mycoplasma pneumoniae Rpr, Rickettsia prowazekii Bbu, Borrelia burgdorferi Bsu, Bacillus subtilis, Hin, Haemophilus influenzae, Hpy, Helicobacter pylori Tma, Thermotoga mari-...

The ribosome recycling factor (RRF) is a 21 kDa protein which is involved in the termination step of protein biosynthesis and catalyses the breakdown of the post termination complex into ribosome, tRNA and mRNA. The solution structure of RRF from the hyperthermophilic bacterium Aquifex aeolicus (7 opt = 85°Q was determined by heteronuclear multidimensional NMR spectroscopy, whereas the backbone NMR assignment was recently carried out for RRF from Themotoga maritima and Thermus thermophilus ... 

A Fe2S2 ferredoxin from the hypertherm ophilic bacterium Aquifex aeolicus, expressed in E. coli, studied by Meyer et al. was shown not to be closely similar to plant or mammalian Fe2S2ferrredoxins.83 The combined EPR, MCD, resonance Raman and Mossbauer study identified an S = state from dithionite reduction with ghvalues of 2.05,1.96 and 1.88. 

With more and more crystal structures becoming available, opinions arise that electrostatic interactions are an important factor conferring thermostability on proteins. This opinion is supported by the increasing number of salt bridges found in many thermostable and hyperthermostable proteins (Table 3.3) (Karshikoff, 2001) comparison of the capsid surface residues in lumazine synthase from Bacillus subtilis (mesophilic) and Aquifex aeolicus (hyperthermophilic) show significantly more charged residues than polar residues in the hyperthermophilic protein. 

Pandelia ME, Nitschke W, Infossi P, Giudici-Orticoni MT, Bill E, Lubitz W. Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus. Proc Nat Acad Sci USA. 2011 108(15) 6097—102. 

Pandelia ME, Infossi P, Stein M, Giudici-Orticoni MT, Lubitz W. Spectroscopic characterization of the key catalytic intermediate Ni-C in the 02-tolerant [NiFe] hydrogenase I from Aquifex aeolicus evidence of a weakly bound hydride. Chem Comm. 2012 48(6) 823-5. 

Pandelia ME, Fourmond V, Tron-Infossi P, et al. Membrane-bound hydrogenase I from the hyperthermophilic bacterium Aquifex aeolicus enzyme activation, redox intermediates and oxygen tolerance. J Am Chem Soc. 2010 132(20) 6991-7004. 

Takata, H., Ohdan, K., Takaha, T., Kuriki, T., and Okada, S. 2003. Properties of branching enzyme from hyperthermophihc bacterium, Aquifex aeolicus, and its potential for production of highly-branched cyclic dextrin. J. Appl. Glycosci., 50, 15-20. 

Thermus aquaticus Thermus thermophilus Thermus filiformis Deinococcus radiodurans Escherichia coli Haemophilus influenzae Streptococus pneumoniae Mycobacterium tuberculosis Mycobacterium laprae Treponema pallidum Chlamydia trachomatis Boriela burgdorferi Helicobacter pyroli Lactococcus lactis Mythelobacterium Rhodothermus obamensis Rickettsia prowazekii Streptomyces coelicolor Bacillus stearothermophilus Synechocystis sp Aquifex aeolicus Apse-1 DNA polymerase T7 DNA polymerase T5 DNA polymerase ... 

In addition to the variations of the GT-A and GT-B fold described above for sialyltransferases (7, 8) and fucosyltrans-ferases (17), a distinct GT-C fold family has been predicted for GTs that use lipid linked donors. The crystal structures of the GT domain of the peptidoglycan glycosyltransferase from Staphylococcus aureus (18) (Fig. 3f) and Aquifex aeolicus, (26) show structural similarity to the bacteriophage k-lysozyme. These novel structures demonstrate the possibility of additional folds. 

Decker G, Warren PV, Gaasterland T, Young WG, Lenox AL, Graham DE, Overbeek R, Snead MA, Keller M, Aujay M, Huber R, Eeldman RA, Short IM, Olsen GJ, Swanson RV. The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature 1998 392 353-358. 

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