2bmb
From Proteopedia
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X-RAY STRUCTURE OF THE BIFUNCTIONAL 6-HYDROXYMETHYL-7,8-DIHYDROXYPTERIN PYROPHOSPHOKINASE DIHYDROPTEROATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE
Overview
In Saccharomyces cerevisiae and other fungi, the enzymes dihydroneopterin, aldolase, 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) and, dihydropteroate synthase (DHPS) are encoded by a polycistronic gene that, is translated into a single polypeptide having all three functions. These, enzymatic functions are essential to both prokaryotes and lower, eukaryotes, and catalyse sequential reactions in folate biosynthesis., Deletion or disruption of either function leads to cell death. These, enzymes are absent from mammals and thus make ideal antimicrobial targets., DHPS is currently the target of antifolate therapy for a number of, infectious diseases, and its activity is inhibited by sulfonamides and, sulfones. These drugs are typically used as part of a synergistic cocktail, ... [(full description)]
About this Structure
2BMB is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with PMM as [ligand]. Full crystallographic information is available from [OCA].
Reference
The three-dimensional structure of the bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/dihydropteroate synthase of Saccharomyces cerevisiae., Lawrence MC, Iliades P, Fernley RT, Berglez J, Pilling PA, Macreadie IG, J Mol Biol. 2005 May 6;348(3):655-70. PMID:15826662
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