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TitleHeterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions.
Journal, issue, pagesPlos One, Vol. 8, Page e81753-e81753, Year 2013
Publish dateAug 16, 2010 (structure data deposition date)
AuthorsArbing, M.A. / Chan, S. / Harris, L. / Kuo, E. / Zhou, T.T. / Ahn, C.J. / Nguyen, L. / He, Q. / Lu, J. / Menchavez, P.T. ...Arbing, M.A. / Chan, S. / Harris, L. / Kuo, E. / Zhou, T.T. / Ahn, C.J. / Nguyen, L. / He, Q. / Lu, J. / Menchavez, P.T. / Shin, A. / Holton, T. / Sawaya, M.R. / Cascio, D. / Eisenberg, D.
External linksPlos One / PubMed:24312350
MethodsX-ray diffraction
Resolution1.956 - 2.7 Å
Structure data

PDB-3ogi:
Crystal structure of the Mycobacterium tuberculosis H37Rv EsxOP complex (Rv2346c-Rv2347c)
Method: X-RAY DIFFRACTION / Resolution: 2.549 Å

PDB-3q4h:
Crystal structure of the Mycobacterium smegmatis EsxGH complex (MSMEG_0620-MSMEG_0621)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-4gzr:
Crystal structure of the Mycobacterium tuberculosis H37Rv EsxOP (Rv2346c-Rv2347c) complex in space group C2221
Method: X-RAY DIFFRACTION / Resolution: 2.553 Å

PDB-4i0x:
Crystal structure of the Mycobacterum abscessus EsxEF (Mab_3112-Mab_3113) complex
Method: X-RAY DIFFRACTION / Resolution: 1.956 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-GOL:
GLYCEROL

Source
  • mycobacterium tuberculosis (bacteria)
  • mycobacterium smegmatis (bacteria)
  • mycobacterium abscessus (bacteria)
KeywordsStructural Genomics / Unknown function / PSI-2 / Protein Structure Initiative / Integrated Center for Structure and Function Innovation / ISFI / TB Structural Genomics Consortium / TBSGC / WXG100 / Secreted / METAL TRANSPORT / 4-helix bundle / WXG100 motif / ESAT-6/ CFP-10 family / ESAT-6-like protein

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