1w4t
From Proteopedia
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|PDB= 1w4t |SIZE=350|CAPTION= <scene name='initialview01'>1w4t</scene>, resolution 1.950Å | |PDB= 1w4t |SIZE=350|CAPTION= <scene name='initialview01'>1w4t</scene>, resolution 1.950Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w4t OCA], [http://www.ebi.ac.uk/pdbsum/1w4t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w4t RCSB]</span> | ||
}} | }} | ||
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[[Category: Sim, E.]] | [[Category: Sim, E.]] | ||
[[Category: Westwood, I M.]] | [[Category: Westwood, I M.]] | ||
| - | [[Category: SO4]] | ||
[[Category: 5-aminosalicylic acid]] | [[Category: 5-aminosalicylic acid]] | ||
[[Category: acyltransferase]] | [[Category: acyltransferase]] | ||
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[[Category: xenobiotic metabolism]] | [[Category: xenobiotic metabolism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:31:12 2008'' |
Revision as of 21:31, 30 March 2008
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| , resolution 1.950Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY CRYSTALLOGRAPHIC STRUCTURE OF PSEUDOMONAS AERUGINOSA ARYLAMINE N-ACETYLTRANSFERASE
Overview
The gene for NAT (arylamine N-acetyltransferase) from Pseudomonas aeruginosa (panat) has been cloned from genomic DNA, and the gene product (PANAT) expressed as an N-terminal histidine-tagged protein in Escherichia coli and purified via nickel ion affinity chromatography. The specific activities of PANAT against a broad range of substrates have been investigated and compared with those of other prokaryotic NAT enzymes. For most arylamine substrates identified, PANAT exhibits in vitro specific activities typically one order of magnitude greater than those of recombinant NAT enzymes from Mycobacterium smegmatis or Salmonella typhimurium. Among the substrates of PANAT so far identified are the anti-tubercular drug isoniazid, 5-aminosalicylate (a drug used in the treatment of inflammatory bowel disease), as well as important environmental pollutants such as 3,4-dichloroaniline and 2-aminofluorene. As well as acetylating common NAT substrates, PANAT is unique among the prokaryotic NATs so far studied in acetylating the folate precursor 4-aminobenzoic acid and the folate catabolite 4-aminobenzoylglutamate. The recombinant protein has been expressed in sufficient quantity to allow protein crystallization, and we have subsequently determined the 1.95 A structure of PANAT by X-ray crystallography.
About this Structure
1W4T is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Expression, purification, characterization and structure of Pseudomonas aeruginosa arylamine N-acetyltransferase., Westwood IM, Holton SJ, Rodrigues-Lima F, Dupret JM, Bhakta S, Noble ME, Sim E, Biochem J. 2005 Jan 15;385(Pt 2):605-12. PMID:15447630
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