1aj2
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(New page: 200px<br /><applet load="1aj2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aj2, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 08:46, 20 November 2007
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CRYSTAL STRUCTURE OF A BINARY COMPLEX OF E. COLI DIHYDROPTEROATE SYNTHASE
Overview
Sulfonamides were amongst the first clinically useful antibacterial agents, to be discovered. The identification of sulfanilamide as the active, component of the dye Prontosil rubrum led to the synthesis of clinically, useful analogues. Today sulfamethoxazole (in combination with, trimethoprim), is used to treat urinary tract infections caused by, bacteria such as Escherichia coli and is also a first-line treatment for, pneumonia caused by the fungus Pneumocystis carinii, a common condition in, AIDS patients. The site of action is the de novo folate biosynthesis, enzyme dihydropteroate synthase (DHPS) where sulfonamides act as analogues, of one of the substrates, para-aminobenzoic acid (pABA). We report here, the crystal structure of E.coli DHPS at 2.0 A resolution refined to an, R-factor of 0.185. The single domain of 282 residues forms an, eight-stranded alpha/beta-barrel. The 7,8-dihydropterin pyrophosphate, (DHPPP) substrate binds in a deep cleft in the barrel, whilst, sulfanilamide binds closer to the surface. The DHPPP ligand site is highly, conserved amongst prokaryotic and eukaryotic DHPSs.
About this Structure
1AJ2 is a Single protein structure of sequence from Escherichia coli with SO4 and 2PH as ligands. Active as Dihydropteroate synthase, with EC number 2.5.1.15 Full crystallographic information is available from OCA.
Reference
Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase., Achari A, Somers DO, Champness JN, Bryant PK, Rosemond J, Stammers DK, Nat Struct Biol. 1997 Jun;4(6):490-7. PMID:9187658
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