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Published on: February 26, 2018
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Substrate-analogue complex structure of Mycobacterium tuberculosis decaprenyl diphosphate synthase
Tzu Ping Ko1, Xiansha Xiao2, Rey Ting Guo3
1Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
Summary
Decaprenyl diphosphate synthase from Mycobacterium tuberculosis (MtDPPS) forms cis double bonds during isoprenoid chain elongation. Structural analysis reveals active site details and suggests strategies for developing MtDPPS inhibitors.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Mycobacterium tuberculosis decпреnyl diphosphate synthase (MtDPPS) elongates farnesyl diphosphate using isoprene units.
- MtDPPS exhibits a butterfly-like homodimer structure, characteristic of cis-type prenyltransferases.
Purpose of the Study:
- To elucidate the active-site configuration and catalytic mechanism of MtDPPS.
- To identify potential strategies for designing MtDPPS inhibitors.
Main Methods:
- X-ray crystallography at 1.55 Å resolution.
- Co-crystallization of MtDPPS with substrate analogues: geranyl S-thiodiphosphate (GSPP) and isopentenyl S-thiodiphosphate.
Main Results:
- Detailed structure of MtDPPS in complex with GSPP and isopentenyl S-thiodiphosphate bound to active sites.
- Visualization of magnesium-coordinated geometry essential for catalysis.
- Evidence for a product translocation pathway from the S2 to the S1 site.
Conclusions:
- The study provides high-resolution structural insights into MtDPPS catalysis.
- Observed effector binding at the S1 site suggests a viable target for inhibitor development.
Keywords:
Mycobacterium tuberculosisRv2361ccatalytic mechanismcell-wall biosynthesiscis-prenyltransferasedecaprenyl diphosphate synthaseinhibitorthiodiphosphateMore Related Videos
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