2v84
From Proteopedia
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CRYSTAL STRUCTURE OF THE TP0655 (TPPOTD) LIPOPROTEIN OF TREPONEMA PALLIDUM
Overview
Tp0655 of Treponema pallidum, the causative agent of syphilis, is, predicted to be a 40 kDa membrane lipoprotein. Previous sequence analysis, of Tp0655 noted its homology to polyamine-binding proteins of the, bacterial PotD family, which serve as periplasmic ligand-binding proteins, of ATP-binding-cassette (ABC) transport systems. Here, the 1.8 A crystal, structure of Tp0655 demonstrated structural homology to Escherichia coli, PotD and PotF. The latter two proteins preferentially bind spermidine and, putrescine, respectively. All of these proteins contain two domains that, sandwich the ligand between them. The ligand-binding site of Tp0655 can be, occupied by 2-(N-morpholino)ethanesulfanoic acid, a component of the, crystallization medium. To discern the polyamine binding preferences of, ... [(full description)]
About this Structure
2V84 is a [Single protein] structure of sequence from [Treponema pallidum] with CL and MES as [ligands]. Full crystallographic information is available from [OCA].
Reference
Structural and Biochemical Basis for Polyamine Binding to the Tp0655 Lipoprotein of Treponema pallidum: Putative Role for Tp0655 (TpPotD) as a Polyamine Receptor., Machius M, Brautigam CA, Tomchick DR, Ward P, Otwinowski Z, Blevins JS, Deka RK, Norgard MV, J Mol Biol. 2007 Aug 21;. PMID:17868688
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