1n71: Difference between revisions

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New page: left|200px<br /><applet load="1n71" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n71, resolution 1.80Å" /> '''Crystal structure of...
 
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[[Image:1n71.gif|left|200px]]<br /><applet load="1n71" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme A'''<br />


==Overview==
==Crystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme A==
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.
<StructureSection load='1n71' size='340' side='right'caption='[[1n71]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
1N71 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium] with SO4 and COA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N71 OCA].  
</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='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>
==Reference==
<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>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12592013 12592013]
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q47764_ENTFC Q47764_ENTFC]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n7/1n71_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>
__TOC__
</StructureSection>
[[Category: Enterococcus faecium]]
[[Category: Enterococcus faecium]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berghuis, A.M.]]
[[Category: Berghuis AM]]
[[Category: Burk, D.L.]]
[[Category: Burk DL]]
[[Category: Ghuman, N.]]
[[Category: Ghuman N]]
[[Category: Wybenga-Groot, L.E.]]
[[Category: Wybenga-Groot LE]]
[[Category: COA]]
[[Category: SO4]]
[[Category: aminoglycoside 6'-n-acetyltransferase]]
[[Category: antibiotic resistance]]
[[Category: coenzyme a]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:39:49 2007''

Latest revision as of 10:53, 14 February 2024

Crystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme ACrystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme A

Structural highlights

1n71 is a 4 chain structure with sequence from Enterococcus faecium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q47764_ENTFC

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1n71, resolution 1.80Å

Drag the structure with the mouse to rotate

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