8avs

Racemic protein crystal structure of aureocin A53 from Staphylococcus aureus in the presence of citrate and acetate

spinqualitylabelsall models 8avs, resolution 1.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8avs is a 4 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.21Å Ligands: ACT, DAL, DGL, DGN, DIL, DLE, DLY, DPN, DPR, DSG, DSN, DTH, DTR, DTY, DVA, EDO, MED, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AUREO_STAAU Publication Abstract from PubMed Tryptophan is frequently found on the surface of membrane-associated proteins that interact with the lipid membrane. However, because of their multifaceted interactions, it is difficult to pinpoint the structure-activity relationship of each tryptophan residue. Here, we describe the use of racemic protein crystallography to probe dedicated tryptophan interactions of a model tryptophan-rich bacteriocin aureocin A53 (AucA) by inclusion and/or exclusion of potential ligands. In the presence of tetrahedral anions that are isosteric to the head group of phospholipids, distinct tryptophan H-bond networks were revealed. H-bond donation by W40 was critical for antibacterial activity, as its substitution by 1-methyltryptophan resulted in substantial loss of activity against bacterial clinical isolates. Meanwhile, exclusion of tetrahedral ions revealed that W3 partakes in formation of a dimeric interface, thus suggesting that AucA is dimeric in solution and dissociated to interact with the phosphate head group in the presence of the lipid membrane. Based on these findings, we could predict the tryptophan residue responsible for activity as well as the oligomeric state of a distant homologue lacticin Q (48%). Roles of inter- and intramolecular tryptophan interactions in membrane-active proteins revealed by racemic protein crystallography.,Lander AJ, Mercado LD, Li X, Taily IM, Findlay BL, Jin Y, Luk LYP Commun Chem. 2023 Jul 18;6(1):154. doi: 10.1038/s42004-023-00953-y. PMID:37464011 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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