8BV9
Acylphosphatase from E. coli
Summary for 8BV9
| Entry DOI | 10.2210/pdb8bv9/pdb |
| Descriptor | Acylphosphatase, GLYCEROL, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | alpha and beta proteins, hydrolase, amyloid, phosphatase, intertwined |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 11794.27 |
| Authors | Gavira, J.A.,Martinez-Rodriguez, S. (deposition date: 2023-01-18, release date: 2023-10-18, Last modification date: 2024-10-23) |
| Primary citation | Martinez-Rodriguez, S.,Camara-Artigas, A.,Gavira, J.A. First 3-D structural evidence of a native-like intertwined dimer in the acylphosphatase family. Biochem.Biophys.Res.Commun., 682:85-90, 2023 Cited by PubMed Abstract: 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-β-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 β-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. PubMed: 37804591DOI: 10.1016/j.bbrc.2023.09.053 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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