| Structural highlights
Function
MMPLB_MYCTU Part of a heme-iron acquisition system. Receives heme from the heme-binding protein Rv0203 and transports it into the mycobacterial cell. Contributes to virulence.[1] [2] [3] Could also transport the mycolic acid-containing lipids monomeromycolyl diacylglycerol (MMDAG) and mycolate ester wax (WE) to the bacterial surface.[4]
References
- ↑ Domenech P, Reed MB, Barry CE 3rd. Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance. Infect Immun. 2005 Jun;73(6):3492-501. PMID:15908378 doi:https://dx.doi.org/10.1128/IAI.73.6.3492-3501.2005
- ↑ Tullius MV, Harmston CA, Owens CP, Chim N, Morse RP, McMath LM, Iniguez A, Kimmey JM, Sawaya MR, Whitelegge JP, Horwitz MA, Goulding CW. Discovery and characterization of a unique mycobacterial heme acquisition system. Proc Natl Acad Sci U S A. 2011 Mar 7. PMID:21383189 doi:10.1073/pnas.1009516108
- ↑ Owens CP, Chim N, Graves AB, Harmston CA, Iniguez A, Contreras H, Liptak MD, Goulding CW. The Mycobacterium tuberculosis secreted protein Rv0203 transfers heme to membrane proteins MmpL3 and MmpL11. J Biol Chem. 2013 Jul 26;288(30):21714-28. doi: 10.1074/jbc.M113.453076. Epub, 2013 Jun 11. PMID:23760277 doi:https://dx.doi.org/10.1074/jbc.M113.453076
- ↑ Pacheco SA, Hsu FF, Powers KM, Purdy GE. MmpL11 protein transports mycolic acid-containing lipids to the mycobacterial cell wall and contributes to biofilm formation in Mycobacterium smegmatis. J Biol Chem. 2013 Aug 16;288(33):24213-22. doi: 10.1074/jbc.M113.473371. Epub, 2013 Jul 8. PMID:23836904 doi:https://dx.doi.org/10.1074/jbc.M113.473371
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