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atcc 700084  (ATCC)


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    Structured Review

    ATCC atcc 700084
    Atcc 700084, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/atcc 700084/product/ATCC
    Average 99 stars, based on 1 article reviews
    atcc 700084 - by Bioz Stars, 2025-02
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    Image Search Results


    a Enc-CD gene organization in prokaryotes. b Phylogenetic tree of Mmp1 proteins and homologs in mycobacteria. Pathogenic mycobacteria and M. smegmatis mc 2 155 are highlighted with the black star and grey star, respectively. The phylogenetic tree was constructed using MEGA11 and annotated with iTOL .

    Journal: Communications Biology

    Article Title: The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin

    doi: 10.1038/s42003-024-07299-8

    Figure Lengend Snippet: a Enc-CD gene organization in prokaryotes. b Phylogenetic tree of Mmp1 proteins and homologs in mycobacteria. Pathogenic mycobacteria and M. smegmatis mc 2 155 are highlighted with the black star and grey star, respectively. The phylogenetic tree was constructed using MEGA11 and annotated with iTOL .

    Article Snippet: The genes were amplified from the genomic DNA of M. smegmatis mc 2 155 (ATCC 700084) and inserted in the frame between ATG start codon and SalI site of the shuttle vector pMV-261 with C-terminal Flag tag fusions to Enc-CD (pMV-261-Enc-CD) or N-terminal Flag tag fusions to Mmp1 (pMV-261-Mmp1-Enc-CD, pMV-261-Mmp1, pMV-261-Mmp1-1-21-CTD, pMV-261-Mmp1-35-55-CTD, pMV-261-Mmp1-107-121-CTD, pMV-261-Mmp1-1-50-CTD, pMV-261-Mmp1-51-155-CTD, and pMV-261-Mmp1-∆1-155-CTD).

    Techniques: Construct

    a The cryo-EM map of holo-Mmp1. The 5, 3, and 2-fold axis are identified by the red pentagon, triangle and oval, respectively. b The cargo densities (gold) within the holo-Mmp1 cavity with the threshold 0.1. c Apo-Mmp1 icosahedral shell ( T = 1) formed from 60 protomers (purple). d The cymbals-like structures from the decameric assembly (red). e The superimposed structures of Mmp1 protomers from the large and small assemblies, with the same coloring scheme as in ( b , c ). f The superimposed structures of the protomers from M. smegmatis Ms CFP-29 ( T = 1), Ms Mmp1 ( T = 1) and M. xanthus Mx EncA ( T = 3). M. smegmatis Ms CFP-29 (PDB 7BOJ), the Ms Mmp1 and M. xanthus Mx EncA (PDB 4PT2) are shown in pink, purple and orange, respectively. g Arrangement of the neighboring protomers as viewed from the 2-fold axis. The interactions networks involved in the 2-fold symmetric interfaces are highlighted in pink, purple and orange, respectively. The CFP-29 forms E-loop interactions networks whereas the Mmp1 ( T = 1) and EncA ( T = 3) does not form connections between E-loops. Mmp1 ( T = 1) uses a chainmail-like topology.

    Journal: Communications Biology

    Article Title: The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin

    doi: 10.1038/s42003-024-07299-8

    Figure Lengend Snippet: a The cryo-EM map of holo-Mmp1. The 5, 3, and 2-fold axis are identified by the red pentagon, triangle and oval, respectively. b The cargo densities (gold) within the holo-Mmp1 cavity with the threshold 0.1. c Apo-Mmp1 icosahedral shell ( T = 1) formed from 60 protomers (purple). d The cymbals-like structures from the decameric assembly (red). e The superimposed structures of Mmp1 protomers from the large and small assemblies, with the same coloring scheme as in ( b , c ). f The superimposed structures of the protomers from M. smegmatis Ms CFP-29 ( T = 1), Ms Mmp1 ( T = 1) and M. xanthus Mx EncA ( T = 3). M. smegmatis Ms CFP-29 (PDB 7BOJ), the Ms Mmp1 and M. xanthus Mx EncA (PDB 4PT2) are shown in pink, purple and orange, respectively. g Arrangement of the neighboring protomers as viewed from the 2-fold axis. The interactions networks involved in the 2-fold symmetric interfaces are highlighted in pink, purple and orange, respectively. The CFP-29 forms E-loop interactions networks whereas the Mmp1 ( T = 1) and EncA ( T = 3) does not form connections between E-loops. Mmp1 ( T = 1) uses a chainmail-like topology.

    Article Snippet: The genes were amplified from the genomic DNA of M. smegmatis mc 2 155 (ATCC 700084) and inserted in the frame between ATG start codon and SalI site of the shuttle vector pMV-261 with C-terminal Flag tag fusions to Enc-CD (pMV-261-Enc-CD) or N-terminal Flag tag fusions to Mmp1 (pMV-261-Mmp1-Enc-CD, pMV-261-Mmp1, pMV-261-Mmp1-1-21-CTD, pMV-261-Mmp1-35-55-CTD, pMV-261-Mmp1-107-121-CTD, pMV-261-Mmp1-1-50-CTD, pMV-261-Mmp1-51-155-CTD, and pMV-261-Mmp1-∆1-155-CTD).

    Techniques: Cryo-EM Sample Prep

    a Predicted structural organization of the Enc-CD. The leading region (LR), middle region (MR) and C-terminal cysteine desulfurase domain (CTD) are indicated by the pink, grey and light green box, respectively. b SEC and SDS-PAGE analysis of the operon Mmp1-∆1-155-CTD, Mmp1-1-50-CTD, Mmp1-51-155-CTD and Mmp1-Enc-CD expression in M. smegmatis mc 2 155. c The subcellular distribution of encapsulated GFP and naked GFP in M. smegmatis mc 2 155 (scale bar = 2.5 μm).

    Journal: Communications Biology

    Article Title: The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin

    doi: 10.1038/s42003-024-07299-8

    Figure Lengend Snippet: a Predicted structural organization of the Enc-CD. The leading region (LR), middle region (MR) and C-terminal cysteine desulfurase domain (CTD) are indicated by the pink, grey and light green box, respectively. b SEC and SDS-PAGE analysis of the operon Mmp1-∆1-155-CTD, Mmp1-1-50-CTD, Mmp1-51-155-CTD and Mmp1-Enc-CD expression in M. smegmatis mc 2 155. c The subcellular distribution of encapsulated GFP and naked GFP in M. smegmatis mc 2 155 (scale bar = 2.5 μm).

    Article Snippet: The genes were amplified from the genomic DNA of M. smegmatis mc 2 155 (ATCC 700084) and inserted in the frame between ATG start codon and SalI site of the shuttle vector pMV-261 with C-terminal Flag tag fusions to Enc-CD (pMV-261-Enc-CD) or N-terminal Flag tag fusions to Mmp1 (pMV-261-Mmp1-Enc-CD, pMV-261-Mmp1, pMV-261-Mmp1-1-21-CTD, pMV-261-Mmp1-35-55-CTD, pMV-261-Mmp1-107-121-CTD, pMV-261-Mmp1-1-50-CTD, pMV-261-Mmp1-51-155-CTD, and pMV-261-Mmp1-∆1-155-CTD).

    Techniques: SDS Page, Expressing

    In addition to cysteine desulfurase from the SUF and ISC system in M. smegmatis mc 2 155, Enc-CD-loaded encapsulin is another cysteine desulfurase for sulfur mobilization. The Mmp1 encapsulin provides a special environment for this to occur. The substrate cysteine enter the lumen of the Mmp1 through the pore of the five-fold axis. The cargo Enc-CD catalyzes the formation of poorly soluble polysulfides bound to hydrophobic sites in the protein and are stored as stable sulfur puncta. In the presence of the reductant, the Enc-CD-loaded encapsulin can release sulfur from sulfur puncta (yellow circles) for sulfur metabolism.

    Journal: Communications Biology

    Article Title: The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin

    doi: 10.1038/s42003-024-07299-8

    Figure Lengend Snippet: In addition to cysteine desulfurase from the SUF and ISC system in M. smegmatis mc 2 155, Enc-CD-loaded encapsulin is another cysteine desulfurase for sulfur mobilization. The Mmp1 encapsulin provides a special environment for this to occur. The substrate cysteine enter the lumen of the Mmp1 through the pore of the five-fold axis. The cargo Enc-CD catalyzes the formation of poorly soluble polysulfides bound to hydrophobic sites in the protein and are stored as stable sulfur puncta. In the presence of the reductant, the Enc-CD-loaded encapsulin can release sulfur from sulfur puncta (yellow circles) for sulfur metabolism.

    Article Snippet: The genes were amplified from the genomic DNA of M. smegmatis mc 2 155 (ATCC 700084) and inserted in the frame between ATG start codon and SalI site of the shuttle vector pMV-261 with C-terminal Flag tag fusions to Enc-CD (pMV-261-Enc-CD) or N-terminal Flag tag fusions to Mmp1 (pMV-261-Mmp1-Enc-CD, pMV-261-Mmp1, pMV-261-Mmp1-1-21-CTD, pMV-261-Mmp1-35-55-CTD, pMV-261-Mmp1-107-121-CTD, pMV-261-Mmp1-1-50-CTD, pMV-261-Mmp1-51-155-CTD, and pMV-261-Mmp1-∆1-155-CTD).

    Techniques: