1aj0: Difference between revisions

Revision as of 16:57, 30 June 2008

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File:1aj0.png

Template:STRUCTURE 1aj0

CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI DIHYDROPTEROATE SYNTHASECRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI DIHYDROPTEROATE SYNTHASE

Template:ABSTRACT PUBMED 9187658

About this StructureAbout this Structure

1AJ0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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-'''CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI DIHYDROPTEROATE SYNTHASE'''
+===CRYSTAL STRUCTURE OF A TERNARY 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9187658}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9187658 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9187658}}
 ==About this Structure==
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 [[Category: Synthase]]
 [[Category: Transferase]]
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