1krr
From Proteopedia
(New page: 200px<br /><applet load="1krr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1krr, resolution 2.5Å" /> '''Galactoside Acetyltra...) |
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| - | [[Image:1krr.gif|left|200px]]<br /><applet load="1krr" size=" | + | [[Image:1krr.gif|left|200px]]<br /><applet load="1krr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1krr, resolution 2.5Å" /> | caption="1krr, resolution 2.5Å" /> | ||
'''Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A'''<br /> | '''Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The galactoside acetyltransferase (thiogalactoside transacetylase) of | + | 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== | ==About this Structure== | ||
| - | 1KRR 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 ACO as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1KRR 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 <scene name='pdbligand=ACO:'>ACO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Galactoside O-acetyltransferase]] | [[Category: Galactoside O-acetyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Olsen, L | + | [[Category: Olsen, L R.]] |
| - | [[Category: Roderick, S | + | [[Category: Roderick, S L.]] |
| - | [[Category: Wang, X | + | [[Category: Wang, X G.]] |
[[Category: ACO]] | [[Category: ACO]] | ||
[[Category: left-handed parallel beta helix]] | [[Category: left-handed parallel beta helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:15 2008'' |
Revision as of 11:37, 21 February 2008
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Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A
Overview
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
1KRR is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Galactoside O-acetyltransferase, with EC number 2.3.1.18 Full crystallographic information is available from OCA.
Reference
Structure of the lac operon galactoside acetyltransferase., Wang XG, Olsen LR, Roderick SL, Structure. 2002 Apr;10(4):581-8. PMID:11937062
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