8bv9 | pdb_00008bv9

Acylphosphatase from E. coli

spinqualitylabelsall models 8bv9, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8bv9 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.55Å Ligands: EDO, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACYP_ECO57 Publication Abstract from PubMed Acylphosphatase (AcP, EC 3.6.1.7) is a small model protein conformed by a ferredoxin-like fold, profoundly studied to get insights into protein folding and aggregation processes. Numerous studies focused on the aggregation and/or amyloidogenic properties of AcPs suggest the importance of edge-beta-strands in the process. In this work, we present the first crystallographic structure of Escherichia coli AcP (EcoAcP), showing notable differences with the only available NMR structure for this enzyme. EcoAcP is crystalised as an intertwined dimer formed by replacing a single C-terminal beta-strand between two protomers, suggesting a flexible character of the C-terminal edge of EcoAcP. Despite numerous works where AcP from different sources have been used as a model system for protein aggregation, our domain-swapped EcoAcP structure is the first 3-D structural evidence of native-like aggregated species for any AcP reported to date, providing clues on molecular determinants unleashing aggregation. First 3-D structural evidence of a native-like intertwined dimer in the acylphosphatase family.,Martinez-Rodriguez S, Camara-Artigas A, Gavira JA Biochem Biophys Res Commun. 2023 Oct 2;682:85-90. doi: , 10.1016/j.bbrc.2023.09.053. PMID:37804591 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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