Dataset Information

Structure and mechanism of CSP secretion pump of ComA for Quorum sensing

ABSTRACT: Cross-linking MS data for 1) ComA Apo form and 2) ComA +ATP form. Purified proteins were cross-linked with DSSO, digested with either trypsin or chymotrypsin, and acquired by MS2-MS3 acquisition method. 2 technical replicates were acquired for each digested sample.

ORGANISM(S): Cellular Organisms

SUBMITTER: Min Luo

PROVIDER: PXD038058 | JPOST Repository | Thu Aug 31 00:00:00 BST 2023

REPOSITORIES: jPOST

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Dataset's files

Source:

			Action	DRS
	20220605_ZS_LM_ComA_postC_dsso_chymotrypsin_R1-calib.pep.XML	Pepxml
	20220605_ZS_LM_ComA_postC_dsso_chymotrypsin_R1.raw	Raw
	20220605_ZS_LM_ComA_postC_dsso_chymotrypsin_R2-calib.pep.XML	Pepxml
	20220605_ZS_LM_ComA_postC_dsso_chymotrypsin_R2.raw	Raw
	20220605_ZS_LM_ComA_postC_dsso_trypsin_R1-calib.pep.XML	Pepxml

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Publications

Structural basis of peptide secretion for Quorum sensing by ComA.

Yu Lin L Xu Xin X Chua Wan-Zhen WZ Feng Hao H Ser Zheng Z Shao Kai K Shi Jian J Wang Yumei Y Li Zongli Z Sobota Radoslaw M RM Sham Lok-To LT Luo Min M

Nature communications 20231107 1

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 ...[more]

PMID: 37935699

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