2v84
From Proteopedia
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- | [[Image:2v84.jpg|left|200px]]<br /><applet load="2v84" size=" | + | [[Image:2v84.jpg|left|200px]]<br /><applet load="2v84" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2v84, resolution 1.78Å" /> | caption="2v84, resolution 1.78Å" /> | ||
'''CRYSTAL STRUCTURE OF THE TP0655 (TPPOTD) LIPOPROTEIN OF TREPONEMA PALLIDUM'''<br /> | '''CRYSTAL STRUCTURE OF THE TP0655 (TPPOTD) LIPOPROTEIN OF TREPONEMA PALLIDUM'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
- | 2V84 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum] with CL and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Cl Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2V84 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Cl Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V84 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: treponema pallidum]] | [[Category: treponema pallidum]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:51:32 2008'' |
Revision as of 10:51, 23 January 2008
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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, Tp0655, the protein was subjected to isothermal titration calorimetric, experiments. The titrations established that Tp0655 binds polyamines, avidly, with a marked preference for putrescine (K(d)=10 nM) over, spermidine (K(d)=430 nM), but the related compounds cadaverine and, spermine did not bind. Structural comparisons and structure-based sequence, analyses provide insights into how polyamine-binding proteins recognize, their ligands. In particular, these comparisons allow the derivation of, rules that may be used to predict the function of other members of the, PotD family. The sequential, structural, and functional homology of Tp0655, to PotD and PotF prompt the conclusion that the former likely is the, polyamine-binding component of an ABC-type polyamine transport system in, T. pallidum. We thus rename Tp0655 as TpPotD. The ramifications of TpPotD, as a polyamine-binding protein to the parasitic strategy of T. pallidum, are discussed.
About this Structure
2V84 is a Single protein structure of sequence from Treponema pallidum with and as ligands. Known structural/functional Site: . 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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