Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis of peptide secretion for Quorum sensing by ComA.
Journal, issue, pages	Nat Commun, Vol. 14, Issue 1, Page 7178, Year 2023
Publish date	Nov 7, 2023
Authors	Lin Yu / Xin Xu / Wan-Zhen Chua / Hao Feng / Zheng Ser / Kai Shao / Jian Shi / Yumei Wang / Zongli Li / Radoslaw M Sobota / Lok-To Sham / Min Luo /
PubMed Abstract	Quorum sensing (QS) is a crucial regulatory mechanism controlling bacterial signalling and holds promise for novel therapies against antimicrobial resistance. In Gram-positive bacteria, such as ...Quorum sensing (QS) is a crucial regulatory mechanism controlling bacterial signalling and holds promise for novel therapies against antimicrobial resistance. In Gram-positive bacteria, such as Streptococcus pneumoniae, ComA is a conserved efflux pump responsible for the maturation and secretion of peptide signals, including the competence-stimulating peptide (CSP), yet its structure and function remain unclear. Here, we functionally characterize ComA as an ABC transporter with high ATP affinity and determined its cryo-EM structures in the presence or absence of CSP or nucleotides. Our findings reveal a network of strong electrostatic interactions unique to ComA at the intracellular gate, a putative binding pocket for two CSP molecules, and negatively charged residues facilitating CSP translocation. Mutations of these residues affect ComA's peptidase activity in-vitro and prevent CSP export in-vivo. We demonstrate that ATP-Mg triggers the outward-facing conformation of ComA for CSP release, rather than ATP alone. Our study provides molecular insights into the QS signal peptide secretion, highlighting potential targets for QS-targeting drugs.
External links	Nat Commun / PubMed:37935699 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 8.2 Å
Structure data	34712 8hf4 EMDB-34712, PDB-8hf4: Cryo-EM structure of nucleotide-bound ComA at outward-facing state with EC gate closed conformation Method: EM (single particle) / Resolution: 2.8 Å 34713 8hf5 EMDB-34713, PDB-8hf5: Cryo-EM structure of nucleotide-bound ComA at outward-facing state with EC gate open conformation Method: EM (single particle) / Resolution: 2.9 Å 34714 8hf6 EMDB-34714, PDB-8hf6: Cryo-EM structure of nucleotide-bound ComA E647Q mutant Method: EM (single particle) / Resolution: 3.1 Å 34715 8hf7 EMDB-34715, PDB-8hf7: Cryo-EM structure of ComA bound to its mature substrate CSP peptide Method: EM (single particle) / Resolution: 3.8 Å EMDB-34716: Cryo-EM structure of ComC bound ComA C17A at inward-facing state Method: EM (single particle) / Resolution: 8.2 Å 36882 8k4b EMDB-36882, PDB-8k4b: Cryo-EM structure of nucleotide-bound ComA with ZinC ion Method: EM (single particle) / Resolution: 3.9 Å 36936 8k7a EMDB-36936, PDB-8k7a: Cryo-EM structure of nucleotide-bound ComA E647Q mutant with Mg2+ Method: EM (single particle) / Resolution: 4.2 Å
Chemicals	ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogueYM ChemComp-MG: Unknown entry ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-ZN: Unknown entry
Source	streptococcus pneumoniae d39 (bacteria) streptococcus streptococcus pneumoniae d39 (bacteria) Streptococcus pneumoniae (bacteria) streptococcus pneumoniae r6 (bacteria)
Keywords	MEMBRANE PROTEIN / TRANSPORT PROTEIN / ABC transport / PCAT / HYDROLASE / TRANSLOCASE / ABC transporter