4qc6

<StructureSection load='4qc6' size='340' side='right' caption='[[4qc6]], [[Resolution|resolution]] 1.30&Aring;' scene=''>

<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>

</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>

<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>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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>

[[Category: Frase, H]]

[[Category: Smith, C A]]

[[Category: Toth, M]]

[[Category: Vakulenko, S B]]

[[Category: Weiss, T M]]

[[Category: Acetylcoenzyme-a]]

[[Category: Acetyltransferase]]

[[Category: Transferase-antibiotic complex]]