1xs5
From Proteopedia
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| - | [[Image:1xs5.gif|left|200px]] | + | [[Image:1xs5.gif|left|200px]] |
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| - | '''The Crystal Structure of Lipoprotein Tp32 from Treponema pallidum''' | + | {{Structure |
| + | |PDB= 1xs5 |SIZE=350|CAPTION= <scene name='initialview01'>1xs5</scene>, resolution 1.85Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MET:METHIONINE'>MET</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= tpn32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160 Treponema pallidum]) | ||
| + | }} | ||
| + | |||
| + | '''The Crystal Structure of Lipoprotein Tp32 from Treponema pallidum''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XS5 is a [ | + | 1XS5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XS5 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15489229 15489229] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Treponema pallidum]] | [[Category: Treponema pallidum]] | ||
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[[Category: periplasmic binding protein]] | [[Category: periplasmic binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:13:51 2008'' |
Revision as of 13:13, 20 March 2008
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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
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