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| | ==Structure of selenomethionyl rTp34 from Treponema pallidum== | | ==Structure of selenomethionyl rTp34 from Treponema pallidum== |
| - | <StructureSection load='2o6c' size='340' side='right' caption='[[2o6c]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='2o6c' size='340' side='right'caption='[[2o6c]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2o6c]] is a 2 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=2O6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O6C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2o6c]] is a 2 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=2O6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O6C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o6d|2o6d]], [[2o6e|2o6e]], [[2o6f|2o6f]]</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=2o6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o6c OCA], [https://pdbe.org/2o6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o6c RCSB], [https://www.ebi.ac.uk/pdbsum/2o6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o6c ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tpd ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o6c OCA], [http://pdbe.org/2o6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o6c RCSB], [http://www.ebi.ac.uk/pdbsum/2o6c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o6c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TA34_TREPA TA34_TREPA]] This antigen is a pathogen-specific membrane immunogen. | + | [https://www.uniprot.org/uniprot/TA34_TREPA TA34_TREPA] This antigen is a pathogen-specific membrane immunogen. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Brautigam, C A]] | + | [[Category: Large Structures]] |
| - | [[Category: Deka, R K]] | + | [[Category: Treponema pallidum]] |
| - | [[Category: Lumpkins, S B]] | + | [[Category: Brautigam CA]] |
| - | [[Category: Machius, M]] | + | [[Category: Deka RK]] |
| - | [[Category: Norgard, M V]] | + | [[Category: Lumpkins SB]] |
| - | [[Category: Tomchick, D R]] | + | [[Category: Machius M]] |
| - | [[Category: Dimer]] | + | [[Category: Norgard MV]] |
| - | [[Category: Ig-fold]] | + | [[Category: Tomchick DR]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Metal-ion binding]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Syphili]]
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| Structural highlights
Function
TA34_TREPA This antigen is a pathogen-specific membrane immunogen.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Tp34 (TP0971) membrane lipoprotein of Treponema pallidum, an obligate human pathogen and the agent of syphilis, was previously reported to have lactoferrin binding properties. Given the non-cultivatable nature of T. pallidum, a structure-to-function approach was pursued to clarify further potential relationships between the Tp34 structural and biochemical properties and its propensity to bind human lactoferrin. The crystal structure of a nonacylated, recombinant form of Tp34 (rTp34), solved to a resolution of 1.9A(,) revealed two metaloccupied binding sites within a dimer; the identity of the ion most likely was zinc. Residues from both of the monomers contributed to the interfacial metal-binding sites; a novel feature was that the delta-sulfur of methionine coordinated the zinc ion. Analytical ultracentrifugation showed that, in solution, rTp34 formed a metal-stabilized dimer and that rTp34 bound human lactoferrin with a stoichiometry of 2:1. Isothermal titration calorimetry further revealed that rTp34 bound human lactoferrin at high (submicromolar) affinity. Finally, membrane topology studies revealed that native Tp34 is not located on the outer surface (outer membrane) of T. pallidum but, rather, is periplasmic. How propensity of Tp34 to bind zinc and the iron-sequestering lactoferrin may relate overall to the biology of T. pallidum infection in humans is discussed.
Crystal structure of the Tp34 (TP0971) lipoprotein of treponema pallidum: implications of its metal-bound state and affinity for human lactoferrin.,Deka RK, Brautigam CA, Tomson FL, Lumpkins SB, Tomchick DR, Machius M, Norgard MV J Biol Chem. 2007 Feb 23;282(8):5944-58. Epub 2006 Dec 27. PMID:17192261[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Deka RK, Brautigam CA, Tomson FL, Lumpkins SB, Tomchick DR, Machius M, Norgard MV. Crystal structure of the Tp34 (TP0971) lipoprotein of treponema pallidum: implications of its metal-bound state and affinity for human lactoferrin. J Biol Chem. 2007 Feb 23;282(8):5944-58. Epub 2006 Dec 27. PMID:17192261 doi:10.1074/jbc.M610215200
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