1tx2

Dihydropteroate Synthetase, With Bound Inhibitor MANIC, From Bacillus anthracis

spinqualitylabelsall models 1tx2, resolution 1.83Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tx2 is a 2 chain structure with sequence from Bacillus anthracis str. a2012. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 680, SO4 Related: 1tws, 1tww, 1twz, 1tx0 Gene: folp (Bacillus anthracis str. A2012) Activity: Dihydropteroate synthase, with EC number 2.5.1.15 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Dihydropterate synthase (DHPS) is the target for the sulfonamide class of antibiotics, but increasing resistance has encouraged the development of new therapeutic agents against this enzyme. One approach is to identify molecules that occupy the pterin binding pocket which is distinct from the pABA binding pocket that binds sulfonamides. Toward this goal, we present five crystal structures of DHPS from Bacillus anthracis, a well-documented bioterrorism agent. Three DHPS structures are already known, but our B. anthracis structures provide new insights into the enzyme mechanism. We show how an arginine side chain mimics the pterin ring in binding within the pterin binding pocket. The structures of two substrate analog complexes and the first structure of a DHPS-product complex offer new insights into the catalytic mechanism and the architecture of the pABA binding pocket. Finally, as an initial step in the development of pterin-based inhibitors, we present the structure of DHPS complexed with 5-nitro-6-methylamino-isocytosine. Crystal structure of 7,8-dihydropteroate synthase from Bacillus anthracis: mechanism and novel inhibitor design.,Babaoglu K, Qi J, Lee RE, White SW Structure. 2004 Sep;12(9):1705-17. PMID:15341734 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dihydropteroate synthase

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