1n71: Difference between revisions

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 ==Crystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme A==
-<StructureSection load='1n71' size='340' side='right' caption='[[1n71]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1n71' size='340' side='right'caption='[[1n71]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n71]] is a 4 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=1N71 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N71 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1n71]] is a 4 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=1N71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N71 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b87|1b87]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1n71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n71 OCA], [http://pdbe.org/1n71 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n71 RCSB], [http://www.ebi.ac.uk/pdbsum/1n71 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n71 ProSAT]</span></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=1n71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n71 OCA], [https://pdbe.org/1n71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n71 RCSB], [https://www.ebi.ac.uk/pdbsum/1n71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n71 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q47764_ENTFC Q47764_ENTFC]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / Line 20: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n71 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The rise of antibiotic resistance as a public health concern has led to increased interest in studying the ways in which bacteria avoid the effects of antibiotics. Enzymatic inactivation by several families of enzymes has been observed to be the predominant mechanism of resistance to aminoglycoside antibiotics such as kanamycin and gentamicin. Despite the importance of acetyltransferases in bacterial resistance to aminoglycoside antibiotics, relatively little is known about their structure and mechanism. Here we report the three-dimensional atomic structure of the aminoglycoside acetyltransferase AAC(6')-Ii in complex with coenzyme A (CoA). This structure unambiguously identifies the physiologically relevant AAC(6')-Ii dimer species, and reveals that the enzyme structure is similar in the AcCoA and CoA bound forms. AAC(6')-Ii is a member of the GCN5-related N-acetyltransferase (GNAT) superfamily of acetyltransferases, a diverse group of enzymes that possess a conserved structural motif, despite low sequence homology. AAC(6')-Ii is also a member of a subset of enzymes in the GNAT superfamily that form multimeric complexes. The dimer arrangements within the multimeric GNAT superfamily members are compared, revealing that AAC(6')-Ii forms a dimer assembly that is different from that observed in the other multimeric GNAT superfamily members. This different assembly may provide insight into the evolutionary processes governing dimer formation.
-X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members.,Burk DL, Ghuman N, Wybenga-Groot LE, Berghuis AM Protein Sci. 2003 Mar;12(3):426-37. PMID:12592013<ref>PMID:12592013</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1n71" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 19434]]
+[[Category: Enterococcus faecium]]
-[[Category: Berghuis, A M]]
+[[Category: Large Structures]]
-[[Category: Burk, D L]]
+[[Category: Berghuis AM]]
-[[Category: Ghuman, N]]
+[[Category: Burk DL]]
-[[Category: Wybenga-Groot, L E]]
+[[Category: Ghuman N]]
-[[Category: Aminoglycoside 6'-n-acetyltransferase]]
+[[Category: Wybenga-Groot LE]]
-[[Category: Antibiotic resistance]]
-[[Category: Coenzyme some]]
-[[Category: Transferase]]