Structure of the carbohydrate binding domain associated with MviN, an essential integral membrane protein in tuberculosis — ASN Events
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  2. Session Twelve - Poster Session D including Happy Hour & Trade Display
  3. Structure of the carbohydrate binding domain associated with MviN, an essential integral membrane protein in tuberculosis

Structure of the carbohydrate binding domain associated with MviN, an essential integral membrane protein in tuberculosis (#432)

Christine L Gee 1 2 , Kadamba G Papavinasasundaram 3 , Nathaniel Echols 2 , James M Holton 4 5 , Christopher M Sassetti 3 6 , Tom Alber 2
  1. Australian Synchrotron, Clayton, VIC, Australia
  2. Molecular and Cell Biology, QB3 Institute, University of California, Berkele, Berkeley, California, USA
  3. Microbiology and Physiological Systems, University of Massachusetts Medical School, Worcester, Massachusetts, USA
  4. Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California, USA
  5. Physical Biosciences, LBNL, Berkeley, California, USA
  6. Howard Hughes Medical Institute, Worcester, USA

Bacterial antibiotic resistance is an emerging global problem, compounded by the lack of newly developed antibiotics. Therefore, research into new antibiotic targets is a high priority. Antibiotic targets are commonly bacterial proteins associated with virulence and/or viability. We are targeting the inner-membrane protein MviN that is required for cell viability most likely through a role in cell wall synthesis 1,2 . Homologs of this protein have been found throughout both Gram negative and positive bacteria but not in humans, which makes MviN a good drug target   In mycobacterium tuberculosis MviN is fused to a pseudokinase and a carbohydrate binding domain (CBD). Here we present features of the crystal structure of the CBD and discuss the clues it provides to the function of MviN.

  1. Sassetti CM, Boyd DH, Rubin EJ.[1] Mol Microbiol. 48, 77-84, (2003)
  2. Gee CL, Papavinasasundaram KG, Blair SR, Baer CE, Falick AM, King DS, Griffin JE, Venghatakrishnan H, Zukauskas A, Wei JR, Dhiman RK, Crick DC, Rubin EJ, Sassetti CM, Alber Science Signalling 5,ra7, (2012)