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6det

From Proteopedia

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Current revision (14:33, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6det' size='340' side='right'caption='[[6det]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='6det' size='340' side='right'caption='[[6det]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6det]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"treponema_vincentii"_(ex_brumpt)_smibert_1984 "treponema vincentii" (ex brumpt) smibert 1984]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DET OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DET FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6det]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_vincentii Treponema vincentii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DET FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<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=6det FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6det OCA], [http://pdbe.org/6det PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6det RCSB], [http://www.ebi.ac.uk/pdbsum/6det PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6det ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6det FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6det OCA], [https://pdbe.org/6det PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6det RCSB], [https://www.ebi.ac.uk/pdbsum/6det PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6det ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/S3MDF0_9SPIR S3MDF0_9SPIR]
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Biophysical and biochemical studies on the lipoproteins and other periplasmic proteins from the spirochetal species Treponema pallidum have yielded numerous insights into the functioning of the organism's peculiar membrane organization, its nutritional requirements, and intermediary metabolism. However, not all T. pallidum proteins have proven to be amenable to biophysical studies. One such recalcitrant protein is Tp0309, a putative polar-amino-acid-binding protein of an ABC transporter system. To gain further information on its possible function, a homolog of the protein from the related species T. vincentii was used as a surrogate. This protein, Tv2483, was crystallized, resulting in the determination of its crystal structure at a resolution of 1.75 A. The protein has a typical fold for a ligand-binding protein, and a single molecule of l-arginine was bound between its two lobes. Differential scanning fluorimetry and isothermal titration calorimetry experiments confirmed that l-arginine bound to the protein with unusually high selectivity. However, further comparison to Tp0309 showed differences in key amino-acid-binding residues may impart an alternate specificity for the T. pallidum protein.
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Biophysical insights into a highly selective l-arginine-binding lipoprotein of a pathogenic treponeme.,Deka RK, Liu WZ, Tso SC, Norgard MV, Brautigam CA Protein Sci. 2018 Dec;27(12):2037-2050. doi: 10.1002/pro.3510. Epub 2018 Oct 27. PMID:30242931<ref>PMID:30242931</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6det" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brautigam, C A]]
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[[Category: Treponema vincentii]]
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[[Category: Norgard, M V]]
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[[Category: Brautigam CA]]
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[[Category: Abc transporter]]
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[[Category: Norgard MV]]
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[[Category: Amino-acid-binding protein]]
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[[Category: Ligand-binding protein]]
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[[Category: Transport protein]]
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Current revision

The crystal structure of Tv2483 bound to L-arginine

PDB ID 6det

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