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[[Image:1kqa.gif|left|200px]]


{{Structure
==GALACTOSIDE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A==
|PDB= 1kqa |SIZE=350|CAPTION= <scene name='initialview01'>1kqa</scene>, resolution 3.20&Aring;
<StructureSection load='1kqa' size='340' side='right'caption='[[1kqa]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>
<table><tr><td colspan='2'>[[1kqa]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KQA FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactoside_O-acetyltransferase Galactoside O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.18 2.3.1.18] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
|GENE= laca ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kqa OCA], [https://pdbe.org/1kqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kqa RCSB], [https://www.ebi.ac.uk/pdbsum/1kqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kqa ProSAT]</span></td></tr>
|RELATEDENTRY=[[1krr|1KRR]], [[1kru|1KRU]], [[1krv|1KRV]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kqa OCA], [http://www.ebi.ac.uk/pdbsum/1kqa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kqa RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/THGA_ECOLI THGA_ECOLI] May assist cellular detoxification by acetylating non-metabolizable pyranosides, thereby preventing their reentry into the cell.
== 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/kq/1kqa_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=1kqa ConSurf].
<div style="clear:both"></div>


'''GALACTOSIDE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A'''
==See Also==
 
*[[Galactoside O-acetyltransferase|Galactoside O-acetyltransferase]]
 
__TOC__
==Overview==
</StructureSection>
The galactoside acetyltransferase (thiogalactoside transacetylase) of Escherichia coli (GAT, LacA, EC 2.3.1.18) is a gene product of the classical lac operon. GAT may assist cellular detoxification by acetylating nonmetabolizable pyranosides, thereby preventing their reentry into the cell. The structure of GAT has been solved in binary complexes with acetyl-CoA or CoA and in ternary complexes with CoA and the nonphysiological acceptor substrates isopropyl beta-D-thiogalactoside (IPTG) or p-nitrophenyl beta-D-galactopyranoside (PNPbetaGal). A hydrophobic cleft that binds the thioisopropyl and p-nitrophenyl aglycones of IPTG and PNPbetaGal may discriminate against substrates with hydrophilic substituents at this position, such as lactose, or inducers of the lac operon. An extended loop projecting from the left-handed parallel beta helix domain contributes His115, which is in position to facilitate attack of the C6-hydroxyl group of the substrate on the thioester.
 
==About this Structure==
1KQA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQA OCA].
 
==Reference==
Structure of the lac operon galactoside acetyltransferase., Wang XG, Olsen LR, Roderick SL, Structure. 2002 Apr;10(4):581-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11937062 11937062]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Galactoside O-acetyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Olsen LR]]
[[Category: Olsen, L R.]]
[[Category: Roderick SL]]
[[Category: Roderick, S L.]]
[[Category: Wang X-G]]
[[Category: Wang, X G.]]
[[Category: left-handed parallel beta helix]]
 
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Retrieved from "https://proteopedia.org/1kqa"