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New page: left|200px<br /><applet load="1kru" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kru, resolution 2.8Å" /> '''Galactoside Acetyltra...
 
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[[Image:1kru.jpg|left|200px]]<br /><applet load="1kru" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1kru, resolution 2.8&Aring;" />
'''Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A'''<br />


==Overview==
==Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A==
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.
<StructureSection load='1kru' size='340' side='right'caption='[[1kru]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== 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/kr/1kru_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=1kru ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1KRU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with COA and IPT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KRU OCA].
*[[Galactoside O-acetyltransferase|Galactoside O-acetyltransferase]]
 
__TOC__
==Reference==
</StructureSection>
Structure of the lac operon galactoside acetyltransferase., Wang XG, Olsen LR, Roderick SL, Structure. 2002 Apr;10(4):581-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=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: COA]]
[[Category: IPT]]
[[Category: left-handed parallel beta helix]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:46:29 2007''

Latest revision as of 07:27, 14 February 2024

Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A

1kru, resolution 2.80Å

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