5e96: Difference between revisions
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==Crystal structure of aminoglycoside 6'-acetyltransferase type Ii== | ==Crystal structure of aminoglycoside 6'-acetyltransferase type Ii== | ||
<StructureSection load='5e96' size='340' side='right' caption='[[5e96]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='5e96' size='340' side='right'caption='[[5e96]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e96]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E96 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5e96]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E96 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id=' | <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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5e96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e96 OCA], [https://pdbe.org/5e96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e96 RCSB], [https://www.ebi.ac.uk/pdbsum/5e96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e96 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q47764_ENTFC Q47764_ENTFC] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Enterococcus faecium]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Baettig OM]] | ||
[[Category: | [[Category: Berghuis AM]] | ||
[[Category: | [[Category: Burk DL]] | ||
[[Category: | [[Category: Shi K]] | ||
Latest revision as of 09:17, 5 July 2023
Crystal structure of aminoglycoside 6'-acetyltransferase type IiCrystal structure of aminoglycoside 6'-acetyltransferase type Ii
Structural highlights
FunctionPublication Abstract from PubMedAn enzyme's inherent structural plasticity is frequently associated with substrate binding, yet detailed structural characterization of flexible proteins remains challenging. This study employs complementary biophysical methods to characterize the partially unfolded structure of substrate-free AAC(6')-Ii, an N-acetyltransferase of the GCN5-related N-acetyltransferase (GNAT) superfamily implicated in conferring broad-spectrum aminoglycoside resistance on Enterococcus faecium. The X-ray crystal structure of AAC(6')-Ii is analyzed to identify relative motions of the structural elements that constitute the dimeric enzyme. Comparison with the previously elucidated crystal structure of AAC(6')-Ii with acetyl coenzyme A (AcCoA) reveals conformational changes that occur upon substrate binding. Our understanding of the enzyme's structural plasticity is further refined with small-angle X-ray scattering and circular dichroism analyses, which together reveal how flexible structural elements impact dimerization and substrate binding. These results clarify the extent of unfolding that AAC(6')-Ii undergoes in the absence of AcCoA and provide a structural connection to previously observed allosteric cooperativity of this enzyme. DATABASE: Structural data are available in the PDB database under the accession number 5E96. Comprehensive characterization of ligand-induced plasticity changes in a dimeric enzyme.,Baettig OM, Shi K, Yachnin BJ, Burk DL, Berghuis AM FEBS J. 2016 Jun 22. doi: 10.1111/febs.13788. PMID:27333541[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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