1xs5

<table><tr><td colspan='2'>[[1xs5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"microspironema_pallidum"_(schaudinn_and_hoffmann_1905)_stiles_and_pfender_1905 "microspironema pallidum" (schaudinn and hoffmann 1905) stiles and pfender 1905]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XS5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XS5 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tpn32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160 "Microspironema pallidum" (Schaudinn and Hoffmann 1905) Stiles and Pfender 1905])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xs5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xs5 OCA], [http://pdbe.org/1xs5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xs5 RCSB], [http://www.ebi.ac.uk/pdbsum/1xs5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xs5 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15489229</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Brautigam, C A]]

[[Category: Deka, R K]]

[[Category: Hagman, K E]]

[[Category: Machius, M]]

[[Category: Neil, L]]

[[Category: Norgard, M V]]

[[Category: Tomchick, D R]]

[[Category: Periplasmic binding protein]]