6i0a

Crystal structure of RlpA SPOR domain from Pseudomonas aeruginosa in complex with nuded glycan obtained by co-crystallization

spinqualitylabelsall models 6i0a, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6i0a is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.3Å Ligands: AMU, AMV, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RLPA_PSEAE Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.[HAMAP-Rule:MF_02071] Publication Abstract from PubMed SPOR domains are widely present in bacterial proteins that recognize cell-wall peptidoglycan strands stripped of the peptide stems. This type of peptidoglycan is enriched in the septal ring as a product of catalysis by cell-wall amidases that participate in the separation of daughter cells during cell division. Here, we document binding of synthetic denuded glycan ligands to the SPOR domain of the lytic transglycosylase RlpA from Pseudomonas aeruginosa (SPOR-RlpA) by mass spectrometry and structural analyses, and demonstrate that indeed the presence of peptide stems in the peptidoglycan abrogates binding. The crystal structures of the SPOR domain, in the apo state and in complex with different synthetic glycan ligands, provide insights into the molecular basis for recognition and delineate a conserved pattern in other SPOR domains. The biological and structural observations presented here are followed up by molecular-dynamics simulations and by exploration of the effect on binding of distinct peptidoglycan modifications. Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division.,Alcorlo M, Dik DA, De Benedetti S, Mahasenan KV, Lee M, Dominguez-Gil T, Hesek D, Lastochkin E, Lopez D, Boggess B, Mobashery S, Hermoso JA Nat Commun. 2019 Dec 5;10(1):5567. doi: 10.1038/s41467-019-13354-4. PMID:31804467 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA