6EXS

Crystal structure of a POT family transporter in complex with thioalcohol conjugated peptide.

Summary for 6EXS

• Entry DOI: 10.2210/pdb6exs/pdb
• Descriptor: Peptide ABC transporter permease, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, 2-[[(2~{R})-2-azanyl-3-[(3~{S})-3-methyl-1-oxidanyl-hexan-3-yl]sulfanyl-propanoyl]amino]ethanoic acid, ... (4 entities in total)
• Functional Keywords: major facilitator superfamily, pot transporter, conjugated peptide ligand, membrane protein
• Biological source: Staphylococcus hominis
• Total number of polymer chains: 1
• Total formula weight: 58749.28

Authors

Minhas, G.S.,Newstead, S. (deposition date: 2017-11-09, release date: 2018-06-27, Last modification date: 2024-01-17)

Primary citation

Minhas, G.S.,Bawdon, D.,Herman, R.,Rudden, M.,Stone, A.P.,James, A.G.,Thomas, G.H.,Newstead, S.
Structural basis of malodour precursor transport in the human axilla.
Elife, 7:-, 2018

PubMed Abstract: Mammals produce volatile odours that convey different types of societal information. In , this is now recognised as body odour, a key chemical component of which is the sulphurous thioalcohol, 3-methyl-3-sulfanylhexan-1-ol (3M3SH). Volatile 3M3SH is produced in the underarm as a result of specific microbial activity, which act on the odourless dipeptide-containing malodour precursor molecule, S-Cys-Gly-3M3SH, secreted in the axilla (underarm) during colonisation. The mechanism by which these bacteria recognise S-Cys-Gly-3M3SH and produce body odour is still poorly understood. Here we report the structural and biochemical basis of bacterial transport of S-Cys-Gly-3M3SH by , which is converted to the sulphurous thioalcohol component 3M3SH in the bacterial cytoplasm, before being released into the environment. Knowledge of the molecular basis of precursor transport, essential for body odour formation, provides a novel opportunity to design specific inhibitors of malodour production in humans.

PubMed: 29966586
DOI: 10.7554/eLife.34995

Experimental method

X-RAY DIFFRACTION (2.5 Å)