1kru

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[[Image:1kru.jpg|left|200px]]
 
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{{Structure
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==Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A==
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|PDB= 1kru |SIZE=350|CAPTION= <scene name='initialview01'>1kru</scene>, resolution 2.8&Aring;
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<StructureSection load='1kru' size='340' side='right'caption='[[1kru]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=IPT:ISOPROPYL-1-BETA-D-THIOGALACTOSIDE'>IPT</scene>
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<table><tr><td colspan='2'>[[1kru]] 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=1KRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KRU FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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|GENE= lacA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<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=IPT:ISOPROPYL-1-BETA-D-THIOGALACTOSIDE'>IPT</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kru OCA], [https://pdbe.org/1kru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kru RCSB], [https://www.ebi.ac.uk/pdbsum/1kru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kru ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1kqa|1KQA]], [[1krr|1KRR]], [[1krv|1KRV]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kru OCA], [http://www.ebi.ac.uk/pdbsum/1kru PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kru RCSB]</span>
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== Function ==
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}}
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kr/1kru_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1kru ConSurf].
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<div style="clear:both"></div>
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'''Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A'''
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==See Also==
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*[[Galactoside O-acetyltransferase|Galactoside O-acetyltransferase]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1KRU 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=1KRU OCA].
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==Reference==
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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]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Galactoside O-acetyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Olsen LR]]
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[[Category: Olsen, L R.]]
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[[Category: Roderick SL]]
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[[Category: Roderick, S L.]]
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[[Category: Wang X-G]]
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[[Category: Wang, X G.]]
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[[Category: left-handed parallel beta helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:52:41 2008''
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Current revision

Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A

PDB ID 1kru

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