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8bv9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Acylphosphatase from E. coli== | |
| + | <StructureSection load='8bv9' size='340' side='right'caption='[[8bv9]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8bv9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BV9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bv9 OCA], [https://pdbe.org/8bv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bv9 RCSB], [https://www.ebi.ac.uk/pdbsum/8bv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bv9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ACYP_ECO57 ACYP_ECO57] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:37804591</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Gavira | + | <div class="pdbe-citations 8bv9" style="background-color:#fffaf0;"></div> |
| - | [[Category: Martinez-Rodriguez | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gavira JA]] | ||
| + | [[Category: Martinez-Rodriguez S]] | ||
Revision as of 14:04, 18 October 2023
Acylphosphatase from E. coli
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