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TitleStructural insights into the transporting and catalyzing mechanism of DltB in LTA D-alanylation.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 3404, Year 2024
Publish dateApr 22, 2024
AuthorsPingfeng Zhang / Zheng Liu /
PubMed AbstractDltB, a model member of the Membrane-Bound O-AcylTransferase (MBOAT) superfamily, plays a crucial role in D-alanylation of the lipoteichoic acid (LTA), a significant component of the cell wall of ...DltB, a model member of the Membrane-Bound O-AcylTransferase (MBOAT) superfamily, plays a crucial role in D-alanylation of the lipoteichoic acid (LTA), a significant component of the cell wall of gram-positive bacteria. This process stabilizes the cell wall structure, influences bacterial virulence, and modulates the host immune response. Despite its significance, the role of DltB is not well understood. Through biochemical analysis and cryo-EM imaging, we discover that Streptococcus thermophilus DltB forms a homo-tetramer on the cell membrane. We further visualize DltB in an apo form, in complex with DltC, and in complex with its inhibitor amsacrine (m-AMSA). Each tetramer features a central hole. The C-tunnel of each protomer faces the intratetramer interface and provides access to the periphery membrane. Each protomer binds a DltC without changing the tetrameric organization. A phosphatidylglycerol (PG) molecule in the substrate-binding site may serve as an LTA carrier. The inhibitor m-AMSA bound to the L-tunnel of each protomer blocks the active site. The tetrameric organization of DltB provides a scaffold for catalyzing D-alanyl transfer and regulating the channel opening and closing. Our findings unveil DltB's dual function in the D-alanylation pathway, and provide insight for targeting DltB as a anti-virulence antibiotic.
External linksNat Commun / PubMed:38649359 / PubMed Central
MethodsEM (single particle)
Resolution3.23 - 3.5 Å
Structure data

36192

8jem

EMDB-36192, PDB-8jem:
DltB tetramer in complex with inhibitor m-AMSA
Method: EM (single particle) / Resolution: 3.23 Å

36194

8jes

EMDB-36194, PDB-8jes:
Cryo-EM structure of DltB homo-tetramer
Method: EM (single particle) / Resolution: 3.42 Å

36207

8jf2

EMDB-36207, PDB-8jf2:
Cryo-EM structure of tetrameric DltB/DltC complex
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-ASW:
N-[4-(acridin-9-ylamino)-3-methoxyphenyl]methanesulfonamide / antineoplastic*YM / Amsacrine

ChemComp-PGT:
(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / phospholipid*YM / Phosphatidylglycerol

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-DGA:
DIACYL GLYCEROL / Diglyceride

Source
  • Streptococcus thermophilus (bacteria)
  • streptococcus thermophilus lmg 18311 (bacteria)
KeywordsMEMBRANE PROTEIN/INHIBITOR / channel; anti-virulence; MBOAT; DltB / MEMBRANE PROTEIN / MEMBRANE PROTEIN-INHIBITOR complex / channel / anti-virulence / MBOAT / DltB / DltB; DltC

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