1xs5
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= tpn32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160 Treponema pallidum]) | |GENE= tpn32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160 Treponema pallidum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xs5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xs5 OCA], [http://www.ebi.ac.uk/pdbsum/1xs5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xs5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Norgard, M V.]] | [[Category: Norgard, M V.]] | ||
[[Category: Tomchick, D R.]] | [[Category: Tomchick, D R.]] | ||
| - | [[Category: MET]] | ||
[[Category: lipoprotein]] | [[Category: lipoprotein]] | ||
[[Category: methionine]] | [[Category: methionine]] | ||
[[Category: periplasmic binding protein]] | [[Category: periplasmic binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:53:55 2008'' |
Revision as of 21:53, 30 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | tpn32 (Treponema pallidum) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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