1xs5: Difference between revisions
New page: left|200px<br /><applet load="1xs5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xs5, resolution 1.85Å" /> '''The Crystal Structur... |
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[[Image:1xs5.gif|left|200px]]<br /><applet load="1xs5" size=" | [[Image:1xs5.gif|left|200px]]<br /><applet load="1xs5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1xs5, resolution 1.85Å" /> | caption="1xs5, resolution 1.85Å" /> | ||
'''The Crystal Structure of Lipoprotein Tp32 from Treponema pallidum'''<br /> | '''The Crystal Structure of Lipoprotein Tp32 from Treponema pallidum'''<br /> | ||
==Overview== | ==Overview== | ||
A structure-to-function approach was undertaken to gain insights into the | 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== | ==About this Structure== | ||
1XS5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum] with MET as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1XS5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum] with <scene name='pdbligand=MET:'>MET</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XS5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Treponema pallidum]] | [[Category: Treponema pallidum]] | ||
[[Category: Brautigam, C | [[Category: Brautigam, C A.]] | ||
[[Category: Deka, R | [[Category: Deka, R K.]] | ||
[[Category: Hagman, K | [[Category: Hagman, K E.]] | ||
[[Category: Machius, M.]] | [[Category: Machius, M.]] | ||
[[Category: Neil, L.]] | [[Category: Neil, L.]] | ||
[[Category: Norgard, M | [[Category: Norgard, M V.]] | ||
[[Category: Tomchick, D | [[Category: Tomchick, D R.]] | ||
[[Category: MET]] | [[Category: MET]] | ||
[[Category: lipoprotein]] | [[Category: lipoprotein]] | ||
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[[Category: periplasmic binding protein]] | [[Category: periplasmic binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:58:08 2008'' | ||
Revision as of 13:58, 21 February 2008
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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 with MET as ligand. 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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