1XS5

The Crystal Structure of Lipoprotein Tp32 from Treponema pallidum

Summary for 1XS5

• Entry DOI: 10.2210/pdb1xs5/pdb
• Descriptor: Membrane lipoprotein TpN32, METHIONINE (3 entities in total)
• Functional Keywords: lipoprotein, periplasmic binding protein, methionine, membrane protein
• Biological source: Treponema pallidum
• Cellular location: Cell membrane; Lipid-anchor (Probable): O07950
• Total number of polymer chains: 1
• Total formula weight: 26637.32

Authors

Deka, R.K.,Neil, L.,Hagman, K.E.,Machius, M.,Tomchick, D.R.,Brautigam, C.A.,Norgard, M.V. (deposition date: 2004-10-18, release date: 2004-11-23, Last modification date: 2024-02-14)

Primary citation

Deka, R.K.,Neil, L.,Hagman, K.E.,Machius, M.,Tomchick, D.R.,Brautigam, C.A.,Norgard, M.V.
Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an L-methionine-binding protein
J.Biol.Chem., 279:55644-55650, 2004

PubMed Abstract: 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.

PubMed: 15489229
DOI: 10.1074/jbc.M409263200

Experimental method

X-RAY DIFFRACTION (1.85 Å)