4qc6: Difference between revisions

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==Crystal structure of aminoglycoside 6'-acetyltransferase-Ie==
==Crystal structure of aminoglycoside 6'-acetyltransferase-Ie==
<StructureSection load='4qc6' size='340' side='right' caption='[[4qc6]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='4qc6' size='340' side='right'caption='[[4qc6]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4qc6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QC6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4qc6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_warneri Staphylococcus warneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QC6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=30N:(3R,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]-3,5,9-TRIHYDROXY-8,8-DIMETHYL-10,14-DIOXO-2,4,6-TRIOXA-11,15-DIAZA-3,5-DIPHOSPHAHEPTADECANE-17-SULFINIC+ACID+3,5-DIOXIDE+(NON-PREFERRED+NAME)'>30N</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KAN:KANAMYCIN+A'>KAN</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]] 1.3&#8491;</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=4qc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qc6 OCA], [http://pdbe.org/4qc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qc6 RCSB], [http://www.ebi.ac.uk/pdbsum/4qc6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qc6 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=30N:(3R,5S,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3,5-diphosphaheptadecane-17-sulfinic+acid+3,5-dioxide+(non-preferred+name)'>30N</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KAN:KANAMYCIN+A'>KAN</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=4qc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qc6 OCA], [https://pdbe.org/4qc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qc6 RCSB], [https://www.ebi.ac.uk/pdbsum/4qc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qc6 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/AACA_STAWA AACA_STAWA]
Broad-spectrum resistance to aminoglycoside antibiotics in clinically important Gram-positive staphylococcal and enterococcal pathogens is primarily conferred by the bifunctional enzyme AAC(6')-Ie-APH(2'')-Ia. This enzyme possesses an N-terminal coenzyme A-dependent acetyltransferase domain [AAC(6')-Ie] and a C-terminal GTP-dependent phosphotransferase domain [APH(2'')-Ia], and together they produce resistance to almost all known aminoglycosides in clinical use. Despite considerable effort over the last two or more decades, structural details of AAC(6')-Ie-APH(2'')-Ia have remained elusive. In a recent breakthrough, the structure of the isolated C-terminal APH(2'')-Ia enzyme was determined as the binary Mg2GDP complex. Here, the high-resolution structure of the N-terminal AAC(6')-Ie enzyme is reported as a ternary kanamycin/coenzyme A abortive complex. The structure of the full-length bifunctional enzyme has subsequently been elucidated based upon small-angle X-ray scattering data using the two crystallographic models. The AAC(6')-Ie enzyme is joined to APH(2'')-Ia by a short, predominantly rigid linker at the N-terminal end of a long alpha-helix. This alpha-helix is in turn intrinsically associated with the N-terminus of APH(2'')-Ia. This structural arrangement supports earlier observations that the presence of the intact alpha-helix is essential to the activity of both functionalities of the full-length AAC(6')-Ie-APH(2'')-Ia enzyme.
 
Structure of the bifunctional aminoglycoside-resistance enzyme AAC(6')-Ie-APH(2'')-Ia revealed by crystallographic and small-angle X-ray scattering analysis.,Smith CA, Toth M, Weiss TM, Frase H, Vakulenko SB Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):2754-64. doi:, 10.1107/S1399004714017635. Epub 2014 Sep 27. PMID:25286858<ref>PMID:25286858</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qc6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Frase, H]]
[[Category: Large Structures]]
[[Category: Smith, C A]]
[[Category: Staphylococcus warneri]]
[[Category: Toth, M]]
[[Category: Frase H]]
[[Category: Vakulenko, S B]]
[[Category: Smith CA]]
[[Category: Weiss, T M]]
[[Category: Toth M]]
[[Category: Acetylcoenzyme-a]]
[[Category: Vakulenko SB]]
[[Category: Acetyltransferase]]
[[Category: Weiss TM]]
[[Category: Aminoglycoside]]
[[Category: Antibiotic resistance]]
[[Category: Gnat family]]
[[Category: Transferase]]
[[Category: Transferase-antibiotic complex]]

Latest revision as of 12:45, 1 March 2024

Crystal structure of aminoglycoside 6'-acetyltransferase-Ie

4qc6, resolution 1.30Å

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