1xs5

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[[Image:1xs5.gif|left|200px]]
[[Image:1xs5.gif|left|200px]]
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{{Structure
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|PDB= 1xs5 |SIZE=350|CAPTION= <scene name='initialview01'>1xs5</scene>, resolution 1.85&Aring;
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The line below this paragraph, containing "STRUCTURE_1xs5", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MET:METHIONINE'>MET</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= tpn32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160 Treponema pallidum])
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|DOMAIN=
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{{STRUCTURE_1xs5| PDB=1xs5 | SCENE= }}
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|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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'''The Crystal Structure of Lipoprotein Tp32 from Treponema pallidum'''
'''The Crystal Structure of Lipoprotein Tp32 from Treponema pallidum'''
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[[Category: Norgard, M V.]]
[[Category: Norgard, M V.]]
[[Category: Tomchick, D R.]]
[[Category: Tomchick, D R.]]
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[[Category: lipoprotein]]
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[[Category: Lipoprotein]]
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[[Category: methionine]]
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[[Category: Methionine]]
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[[Category: periplasmic binding protein]]
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[[Category: Periplasmic binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:26:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:53:55 2008''
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Revision as of 12:26, 3 May 2008

Template:STRUCTURE 1xs5

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 Sat May 3 15:26:36 2008

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