2fqw: Difference between revisions

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==PnrA from Treponema pallidum as purified from E. coli (bound to inosine)==
==PnrA from Treponema pallidum as purified from E. coli (bound to inosine)==
<StructureSection load='2fqw' size='340' side='right' caption='[[2fqw]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
<StructureSection load='2fqw' size='340' side='right'caption='[[2fqw]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fqw]] is a 1 chain structure with 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=2FQW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FQW FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fqw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FQW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NOS:INOSINE'>NOS</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.71&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fqx|2fqx]], [[2fqy|2fqy]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NOS:INOSINE'>NOS</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tmpC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160 Treponema pallidum])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fqw OCA], [https://pdbe.org/2fqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fqw RCSB], [https://www.ebi.ac.uk/pdbsum/2fqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fqw ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fqw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fqw RCSB], [http://www.ebi.ac.uk/pdbsum/2fqw PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TMPC_TREPA TMPC_TREPA]] Binds purine nucleosides and may play a role in purine nucleoside uptake. May be part of an ABC-type nucleoside uptake system. Has highest affinity for guanosine, followed by inosine and adenosine. Has very low affinity for cytidine and does not bind thymidine.<ref>PMID:16418175</ref>
[https://www.uniprot.org/uniprot/TMPC_TREPA TMPC_TREPA] Binds purine nucleosides and may play a role in purine nucleoside uptake. May be part of an ABC-type nucleoside uptake system. Has highest affinity for guanosine, followed by inosine and adenosine. Has very low affinity for cytidine and does not bind thymidine.<ref>PMID:16418175</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/2fqw_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/2fqw_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fqw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Treponema pallidum, the bacterial agent of syphilis, cannot be cultivated in vitro. This constraint has severely impeded the study of the membrane biology of this complex human pathogen. A structure-to-function approach thus was adopted as a means of discerning the likely function of Tp0319, a 35-kDa cytoplasmic membrane-associated lipoprotein of T. pallidum formerly designated as TmpC. A 1.7-A crystal structure showed that recombinant Tp0319 (rTp0319) consists of two alpha/beta domains, linked by three crossovers, with a deep cleft between them akin to ATP-binding cassette (ABC) receptors. In the cleft, a molecule of inosine was bound. Isothermal titration calorimetry demonstrated that rTp0319 specifically binds purine nucleosides (dissociation constant (Kd) approximately 10(-7) M). This predilection for purine nucleosides by rTp0319 is consistent with its likely role as a receptor component of a cytoplasmic membrane-associated transporter system. Reverse transcription-PCR analysis of RNA isolated from rabbit tissue-extracted T. pallidum additionally showed that tp0319 is transcriptionally linked to four other downstream open reading frames, thereby supporting the existence of an ABC-like operon (tp0319-0323). We herein thus re-name tp0319 as purine nucleoside receptor A (pnrA), with its operonic partners tp0320-0323 designated as pnrB-E, respectively. Our study not only infers that PnrA transports purine nucleosides essential for the survival of T. pallidum within its obligate human host, but to our knowledge, this is the first description of an ABC-type nucleoside transport system in any bacterium. PnrA has been grouped with a functionally uncharacterized protein family (HBG016869), thereby implying that other members of the family may have similar nucleoside-binding function(s).
The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-like operon in Treponema pallidum.,Deka RK, Brautigam CA, Yang XF, Blevins JS, Machius M, Tomchick DR, Norgard MV J Biol Chem. 2006 Mar 24;281(12):8072-81. Epub 2006 Jan 16. PMID:16418175<ref>PMID:16418175</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Treponema pallidum]]
[[Category: Treponema pallidum]]
[[Category: Brautigam, C A]]
[[Category: Brautigam CA]]
[[Category: Deka, R K]]
[[Category: Deka RK]]
[[Category: Machius, M]]
[[Category: Machius M]]
[[Category: Norgard, M V]]
[[Category: Norgard MV]]
[[Category: Tomchick, D R]]
[[Category: Tomchick DR]]
[[Category: Abc transport system]]
[[Category: Inosine]]
[[Category: Ligand-binding protein]]
[[Category: Transport protein]]
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