Streptomyce lividans

Xylanase (from Streptomyces lividans) [37278-89-0] Mr 43,000 [EC 3.2.1.8]. Purified by anion-exchange chromatography on an Accell QMA column and finally by HPLC using a ProteinPak DEAE 5PW anion-exchange column. Solutions were stored frozen at -70°. [Morosoli et al. Biochem J 239 587 79S6 Wong et al. Microbiol Rev 52 305 1988.]... 

Some metals can be converted to a less toxic form through enzyme detoxification. The most well-described example of this mechanism is the mercury resistance system, which occurs in S. aureus,43 Bacillus sp.,44 E. coli,45 Streptomyces lividans,46 and Thiobacillus ferrooxidans 47 The mer operon in these bacteria includes two different metal resistance mechanisms.48 MerA employs an enzyme detoxification approach as it encodes a mercury reductase, which converts the divalent mercury cation into elemental mercury 49 Elemental mercury is more stable and less toxic than the divalent cation. Other genes in the operon encode membrane proteins that are involved in the active transport of elemental mercury out of the cell.50 52... 

Sedlmeier, R. and Altenbuchner, J., Cloning and DNA sequence analysis of the mercury resistance genes of Streptomyces lividans, Mol Gen Genet, 236 (1), 76-85, 1992. 

Avignone Rossa, C., White, J., Kuiper, A. et al. (2002) Carbon flux distribution in antibiotic-producing chemostat cultures of Streptomyces lividans. Metabolic engineering, 4, 138—150. 

Butler, M.J., Bruheim, P, Jovetic, S. et al. (2002) Engineering of primary carbon metabolism for improved antibiotic production in Streptomyces lividans. Applied and Environmental Microbiology, 68, 4731 4739. 

Streptomyces lividans Voltage- K -channei 2IH1, 2.40 21 2006 Open ... 

The Shaker potassium channel did not yield crystals for the first potassium ion channel X-ray crystallographic structure. Rather, it was the prokaryote bacterium Streptomyces lividans, abbreviated as the KcsA K+ channel, that first produced crystals suitable for crystallography. This structure, published in 1998 by MacKinnon s group in Science magazine, was received with great praise from the scientific community. It was known at that time that the amino acid sequence of KcsA was similar to that of other K channels, including vertebrate and invertebrate voltage-dependent K (Kv) channels (such as the... 

Kim E-S, Hong H-J, Choi C-Y, Cohen SN, Modulation of actinorhodin biosynthesis in Streptomyces lividans by glucose repression of afsR2 gene transcription,... 

The DesVll desosaminyl transferase naturally transfers D-desosamine to both 12- and 14-membered macrolactones, which is an example of inherent flexibility towards the acceptor aglycone. This unusual property of DesVll has been exploited to generate novel macrolide derivatives that differ in size of the macrolactone ring and in their oxygenation/reduction state. A Streptomyces lividans strain in which the genes involved in the biosynthesis and transfer of D-desosamine were... 

Highly resolved structural information is currently available only for a constitutively open channel from Streptomyces lividans (see 16.3.3). 

The successful crystallization and structural determination of the constitutively open charmel of Streptomyces lividans (Doyle et al., 1998) represented a large step forward in the understanding of function and selectivity of ion channels. 

It is to be expected that these basic principles of ion selectivity and ion conduction for the charmel of Streptomyces lividans also apply to other types of ion charmels. 

Fig. 16.6. Schematic view of the K channel from Streptomyces lividans...

KcsA is a potassium channel protein from Streptomyces lividans that assembles as a tetramer.68 An X-ray diffraction study of a crystal defined the transmembrane and some extracellular portions of the structure but no structural information could be obtained for cytoplasmic domains. Since the protein assembles as a tetramer, when one spin label is present on each subunit, it is difficult to interpret the dipolar interactions because of the presence of adjacent... 

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