1xs5
From Proteopedia
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| , resolution 1.85Å | |||||||
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| Ligands: | |||||||
| Gene: | tpn32 (Treponema pallidum) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 15:13:51 2008
