Pseudomonas aeruginosa structure

Fiilop V, Ridout CJ, Greenwood C et al (1995) Crystal-structure of the di-heme cytochrome-c peroxidase from Pseudomonas aeruginosa. Structure 3 1225-1233... 

Nurizzo, D., Silvestrini, M.-C., Mathieu, M., Cutruzzola, E., Bourgeois, D., E,fp, V., Hajdu, J., Brunori, M., Tegoni, M., and Cambillau, C., 1997, N-terminal arm exchange is observed in the 2.15 crystal structure of oxidised nitrite reductase from Pseudomonas aeruginosa. Structure 5 115791171. 

Boumann, U., et al. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa, a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 12 3357-3364, 1993. 

Antholine, W.E., Hanna, P.M., and McMillan, D.R. 1993. Low frequency EPR of Pseudomonas aeruginosa azurin analysis of ligand superhyperfine structure from a type 1 copper site. Biophysical Journal 64 267-272. 

Table 5.2 contains data about selected copper enzymes from the references noted. It should be understood that enzymes from different sources—that is, azurin from Alcaligenes denitrificans versus Pseudomonas aeruginosa, fungal versus tree laccase, or arthropodan versus molluscan hemocyanin—will differ from each other to various degrees. Azurins have similar tertiary structures—in contrast to arthropodan and molluscan hemocyanins, whose tertiary and quaternary structures show large deviations. Most copper enzymes contain one type of copper center, but laccase, ascorbate oxidase, and ceruloplasmin contain Type I, Type II, and Type III centers. For a more complete and specific listing of copper enzyme properties, see, for instance, the review article by Solomon et al.4... 

The first structures of this kind were reported in 1993 pectate lyase G from Erwinia chrysanthemi (Yoder et al, 1993) and alkaline protease from Pseudomonas aeruginosa (Baumann et al, 1993). Based on consideration of these crystal structures, the term parallel //-helix was introduced for a fold containing three //-strands per coil, and parallel //-roll for a fold with two //-strands per coil (Baumann etal, 1993 Yoder andjurnak, 1995 Yoder et al., 1993). The epithet parallel was intended to emphasize the distinction between these folds and the previously observed helical structure of the antibiotic gramicidin which contains both l- and D-amino acids and... 

Fig. 11.—Chemical structure of the two preponderant lipid A forms of Pseudomonas aeruginosa. (A) Pentaacyl lipid A (major lipid A fraction 75%, w/w). (B) Hexaacyl lipid A (minor lipid A fraction, 25%, w/w). Dashed lines indicate nonstoichiometric a-hydroxylation of 12 0. A lipid A species having 2 mol 12 0(2-OH)/mol lipid A was not detected (77).

Figure 2 X-Ray structure of the site active of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa...

Figure 39 X-Ray structure of the copper centre in azurin from Pseudomonas Aeruginosa...

Some less-than-rapid methods may also be considered in process if they are used to modify or enhance the process. Cheung et al. did some work in examining alterations in extracellular substances during biofilm development of Pseudomonas aeruginosa on aluminum plates.25 The FT-IR spectra, taken over days, showed changes by the fifth day. They believe that structural changes or... 

Intramolecular Ru(II) to Cu(II) ET rates have been measured in two other blue copper proteins, stellacyanin [42, 43] and azurin [9, 13, 28]. Pseudomonas aeruginosa azurin has been ruthenated at His83 [13] (Fig. 5). The intramolecular Ru(II) to Cu(II) ET rate of 1.9 s was found to be independent of temperature [28]. The Cu reorganization enthalpy was estimated to be < 7 kcal/mol [13, 28], a value confirming that blue copper is structured for efficient ET. Again, a blue copper ET rate is low in comparison with heme protein rates over similar distances (at similar driving forces) (Table 1). 

Fig. 2. Pyoverdins from Pseudomonas aeruginosa representing the three structural types...

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