1krr
From Proteopedia
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|PDB= 1krr |SIZE=350|CAPTION= <scene name='initialview01'>1krr</scene>, resolution 2.5Å | |PDB= 1krr |SIZE=350|CAPTION= <scene name='initialview01'>1krr</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACO:ACETYL COENZYME *A'>ACO</scene> | + | |LIGAND= <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= lacA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= lacA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1kqa|1KQA]], [[1kru|1KRU]], [[1krv|1KRV]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1krr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1krr OCA], [http://www.ebi.ac.uk/pdbsum/1krr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1krr RCSB]</span> | ||
}} | }} | ||
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[[Category: Roderick, S L.]] | [[Category: Roderick, S L.]] | ||
[[Category: Wang, X G.]] | [[Category: Wang, X G.]] | ||
| - | [[Category: ACO]] | ||
[[Category: left-handed parallel beta helix]] | [[Category: left-handed parallel beta helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:52:38 2008'' |
Revision as of 18:52, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | lacA (Escherichia coli) | ||||||
| Activity: | Galactoside O-acetyltransferase, with EC number 2.3.1.18 | ||||||
| Related: | 1KQA, 1KRU, 1KRV
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 21:52:38 2008
