Bacterial transferases

Bacterial transferases flat trimeric /8-solenoids with T-type cross section... 

Fig. 5. Axial projections of /1-solenoid trimers formed by lateral, in-register, association of the individual solenoids. Only one coil of each solenoid is shown. Different subunits of a trimer are colored in different colors. Ligands of the bacterial transferase are shown in green.

Several /i-solenoid domains appear to promote the oligomerization of multidomain proteins. There are at least three types of /i-solenoid association. First, oligomers (dimers or trimers) are formed by lateral interaction of the solenoids. For example, the C-terminal domain of the bacterial cell division inhibitor MinC is a short right-handed T-type solenoid with an apolar lateral face that mediates homodimerization (Cordell et al., 2001). Trimers of several bacterial transferases are formed by lateral, in-register, interaction of left-handed T-type /1-solenoids (Fig. 5). Second, dimers may form via interactions of the open terminal coils of /1-solenoids as in the dimeric structure of iron transporter stabilizer SufD (Badger et al., 2005). Finally, dimerization may be mediated by swapping of /1-strands of the terminal coils, as in the CAP (Dodatko et al., 2004) (Fig. S). 

Structures of several important aminoglycoside antibiotics. Ring II is 2-deoxystreptamine. The resemblance between kanamycin and amikacin and between gentamicin, netilmicin, and tobramycin can be seen. The circled numerals on the kanamycin molecule indicate points of attack of plasmid-mediated bacterial transferase enzymes that can inactivate this drug. , , and , acetyltransferase , phosphotransferase , adenylyltransferase. Amikacin is resistant to modification at , , , and . 

SxxK free-standing penicillin-binding proteins (PBPs) are uncoupled SxxK acyl transferases that work mainly as bacterial wall peptidoglycan-hydrolases and function as auxiliary cell-cycle proteins. They are not essential. 

Bacterial ribosome function Aminoglycosides Tetracyclines Chloramphenicol Macrolides, azalides Fusidic acid Mupirocin Distort SOS ribosomal subunit Block SOS ribosomal subunit Inhibits peptidyl transferase Block translocation Inhibits elongation factor Inhibits isoleucyl-tRNA synthesis No action on 40S subunit Excluded by mammalian cells No action on mammalian equivalent No action on mammalian equivalent Excluded by mammalian cells No action on mammalian equivalent... 

Coleman NV, JC Spain (2003) Epoxyalkane coenzyme M transferase in the ethene and vinyl chloride biodegradation pathways of Mycobacterium strain JS60. J Bacterial 185 5536-5546. 

Fortin PD, GP Horsman, HM Yang, LD Eltis (2006) A glutathione S-transferase catalyzes the debalogenation of inhibitory metabolites of polychlorinated biphenyls. J Bacterial 188 4424-4430. 

Lloyd-Jones G, PCK Lau (1997) Glutathione 5-transferase-encoding gene as a potential probe for environmental bacterial isolates capable of degrading polycyclic aromatic hydrocarbons. Appl Environ Microbiol 63 3286-3290. 

EPEC = Enteropathogenic E. coli NA = not applicable UTI = urinary tract infections AST = aspartate amino transferase. Indicates studies that documented a substantial number of cases of bacterial diarrhea denotes studies with substantial isolation of bacterial enteropatho-gens. 1 Nonclassic enteric flora includes E. coli with the designation of enteropathogenic E. coli or other recognized diarrheogenic E. coli, Klebsiella, Proteus, Entero- bacter, Pseudomonas and Enterococcus. ... 

Histidine is a low molecular weight chelator considered to be important for the chelation of Ni (Kerkeb and Kramer, 2003). Its synthesis is limited by the enzyme ATP phosphoribosyl transferase, APRT. Transgenic A. thaliana plants over-expressing tHisG (a bacterial APRT) developed increased histidine levels and resulted in an enhanced Ni tolerance without affecting Ni accumulation (Wycisk et al., 2004). 

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