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


{{Structure
==Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal==
|PDB= 1krv |SIZE=350|CAPTION= <scene name='initialview01'>1krv</scene>, resolution 2.80&Aring;
<StructureSection load='1krv' size='340' side='right'caption='[[1krv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=147:1-O-[P-NITROPHENYL]-BETA-D-GALACTOPYRANOSE'>147</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>
<table><tr><td colspan='2'>[[1krv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The March 2003 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''lac Repressor''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2003_3 10.2210/rcsb_pdb/mom_2003_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KRV 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]] 2.8&#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=147:1-O-[P-NITROPHENYL]-BETA-D-GALACTOPYRANOSE'>147</scene>, <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=1krv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1krv OCA], [https://pdbe.org/1krv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1krv RCSB], [https://www.ebi.ac.uk/pdbsum/1krv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1krv ProSAT]</span></td></tr>
|RELATEDENTRY=[[1kqa|1KQA]], [[1krr|1KRR]], [[1kru|1KRU]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1krv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1krv OCA], [http://www.ebi.ac.uk/pdbsum/1krv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1krv 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/kr/1krv_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=1krv ConSurf].
<div style="clear:both"></div>


'''Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal'''
==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==
1KRV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1KRV with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb39_1.html lac Repressor]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRV 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: RCSB PDB Molecule of the Month]]
[[Category: lac Repressor]]
[[Category: Lac Repressor]]
[[Category: Olsen, L R.]]
[[Category: Olsen LR]]
[[Category: Roderick, S L.]]
[[Category: Roderick SL]]
[[Category: Wang, X G.]]
[[Category: Wang X-G]]
[[Category: left-handed parallel beta helix]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:52:43 2008''

Latest revision as of 07:27, 14 February 2024

Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal

1krv, resolution 2.80Å

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