1krv: Difference between revisions

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[[Image:1krv.png|left|200px]]
==Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal==
<StructureSection load='1krv' size='340' side='right' caption='[[1krv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1krv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The March 2003 RCSB PDB [http://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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KRV FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=147:1-O-[P-NITROPHENYL]-BETA-D-GALACTOPYRANOSE'>147</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kqa|1kqa]], [[1krr|1krr]], [[1kru|1kru]]</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lacA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1krv RCSB], [http://www.ebi.ac.uk/pdbsum/1krv PDBsum]</span></td></tr>
<table>
== 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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_1krv|  PDB=1krv  |  SCENE=  }}
Structure of the lac operon galactoside acetyltransferase.,Wang XG, Olsen LR, Roderick SL Structure. 2002 Apr;10(4):581-8. PMID:11937062<ref>PMID:11937062</ref>


===Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_11937062}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1krv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The March 2003 RCSB PDB [http://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 [http://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].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:011937062</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Galactoside O-acetyltransferase]]
[[Category: Galactoside O-acetyltransferase]]

Revision as of 19:08, 28 September 2014

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

Structural highlights

1krv is a 3 chain structure with sequence from Escherichia coli. The March 2003 RCSB PDB Molecule of the Month feature on lac Repressor by David S. Goodsell is 10.2210/rcsb_pdb/mom_2003_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Related:1kqa, 1krr, 1kru
Gene:lacA (Escherichia coli)
Activity:Galactoside O-acetyltransferase, with EC number 2.3.1.18
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

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

Publication Abstract from PubMed

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.

Structure of the lac operon galactoside acetyltransferase.,Wang XG, Olsen LR, Roderick SL Structure. 2002 Apr;10(4):581-8. PMID:11937062[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Wang XG, Olsen LR, Roderick SL. Structure of the lac operon galactoside acetyltransferase. Structure. 2002 Apr;10(4):581-8. PMID:11937062

1krv, resolution 2.80Å

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