4qc6: Difference between revisions
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''' | ==Crystal structure of aminoglycoside 6'-acetyltransferase-Ie== | ||
<StructureSection load='4qc6' size='340' side='right' caption='[[4qc6]], [[Resolution|resolution]] 1.30Å' scene=''> | |||
== 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> | |||
</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://www.rcsb.org/pdb/explore.do?structureId=4qc6 RCSB], [http://www.ebi.ac.uk/pdbsum/4qc6 PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Frase, H.]] | |||
[[Category: Smith, C A.]] | |||
[[Category: Toth, M.]] | |||
[[Category: Vakulenko, S B.]] | |||
[[Category: Weiss, T M.]] | |||
[[Category: Acetylcoenzyme-a]] | |||
[[Category: Acetyltransferase]] | |||
[[Category: Aminoglycoside]] | |||
[[Category: Antibiotic resistance]] | |||
[[Category: Gnat family]] | |||
[[Category: Transferase]] | |||
[[Category: Transferase-antibiotic complex]] | |||
Revision as of 11:44, 22 October 2014
Crystal structure of aminoglycoside 6'-acetyltransferase-Ie
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