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| | <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 with sequence from [http://en.wikipedia.org/wiki/Atcc_19434 Atcc 19434]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E96 FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1n71|1n71]], [[1b87|1b87]]</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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aac(6 )-II ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1352 ATCC 19434])</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=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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5e96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e96 OCA], [http://pdbe.org/5e96 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e96 RCSB], [http://www.ebi.ac.uk/pdbsum/5e96 PDBsum], [http://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: Atcc 19434]] | + | [[Category: Enterococcus faecium]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baettig, O M]] | + | [[Category: Baettig OM]] |
| - | [[Category: Berghuis, A M]] | + | [[Category: Berghuis AM]] |
| - | [[Category: Burk, D L]] | + | [[Category: Burk DL]] |
| - | [[Category: Shi, K]] | + | [[Category: Shi K]] |
| - | [[Category: Acetyltransferase]]
| + | |
| - | [[Category: Aminoglycoside resistance]]
| + | |
| - | [[Category: Gnat]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q47764_ENTFC
Publication Abstract from PubMed
An 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
- ↑ Baettig OM, Shi K, Yachnin BJ, Burk DL, Berghuis AM. Comprehensive characterization of ligand-induced plasticity changes in a dimeric enzyme. FEBS J. 2016 Jun 22. doi: 10.1111/febs.13788. PMID:27333541 doi:http://dx.doi.org/10.1111/febs.13788
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