1xs5
From Proteopedia
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The Crystal Structure of Lipoprotein Tp32 from Treponema pallidum
Overview
A structure-to-function approach was undertaken to gain insights into the, potential function of the 32-kDa membrane lipoprotein (Tp32) of Treponema, pallidum, the syphilis bacterium. The crystal structure of rTp32, (determined at a resolution of 1.85 A) shows that the organization of, rTp32 is similar to other periplasmic ligand-binding proteins (PLBPs), in, that it consists of two alpha/beta domains, linked by two crossovers, with, a binding pocket between them. In the pocket, a molecule of L-methionine, was detected in the electron density map. Residues from both domains, interact with the ligand. One of the crossover regions is comprised of a, 3(10)-helix, a feature not typical in other ligand-binding proteins., Sequence comparison shows strong similarity to other hypothetical, methionine-binding proteins. Together, the data support the notion that, rTp32 is a component of a periplasmic methionine uptake transporter system, in T. pallidum.
About this Structure
1XS5 is a Single protein structure of sequence from Treponema pallidum with MET as ligand. Full crystallographic information is available from OCA.
Reference
Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an L-methionine-binding protein., Deka RK, Neil L, Hagman KE, Machius M, Tomchick DR, Brautigam CA, Norgard MV, J Biol Chem. 2004 Dec 31;279(53):55644-50. Epub 2004 Oct 15. PMID:15489229
Page seeded by OCA on Wed Nov 21 06:18:39 2007
