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| | <StructureSection load='1us4' size='340' side='right'caption='[[1us4]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='1us4' size='340' side='right'caption='[[1us4]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1us4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1US4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1US4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1us4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1US4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1US4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</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]] 1.75Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1us5|1us5]]</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=1us4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1us4 OCA], [https://pdbe.org/1us4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1us4 RCSB], [https://www.ebi.ac.uk/pdbsum/1us4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1us4 ProSAT], [https://www.topsan.org/Proteins/RSGI/1us4 TOPSAN]</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=1us4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1us4 OCA], [http://pdbe.org/1us4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1us4 RCSB], [http://www.ebi.ac.uk/pdbsum/1us4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1us4 ProSAT], [http://www.topsan.org/Proteins/RSGI/1us4 TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/P83817_THETH P83817_THETH] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet8]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Inagaki, E]] | + | [[Category: Inagaki E]] |
| - | [[Category: Tahirov, T H]] | + | [[Category: Tahirov TH]] |
| - | [[Category: Takahashi, H]] | + | [[Category: Takahashi H]] |
| - | [[Category: Glur0]]
| + | |
| - | [[Category: Glutamate receptor]]
| + | |
| - | [[Category: L-glutamate]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| Structural highlights
Function
P83817_THETH
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
As part of a structural genomics project, the crystal structure of a 314-amino-acid protein encoded by Thermus thermophilus HB8 gene TT1099 was solved to 1.75 A using the multiple-wavelength anomalous dispersion (MAD) method and a selenomethionine-incorporated protein. The native protein structure was solved to 1.5 A using the molecular-replacement method. Both structures revealed a bound ligand, L-glutamate or L-glutamine, and a fold related to the periplasmic substrate-binding proteins (PSBP). Further comparative structural analysis with other PSBP-fold proteins revealed the conservation of the predicted membrane permease binding surface area and indicated that the T. thermophilus HB8 molecule is most likely to be an L-glutamate and/or an L-glutamine-binding protein related to the cluster 3 periplasmic receptors. However, the geometry of ligand binding is unique to the T. thermophilus HB8 molecule.
Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein.,Takahashi H, Inagaki E, Kuroishi C, Tahirov TH Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1846-54. Epub 2004, Sep 23. PMID:15388932[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takahashi H, Inagaki E, Kuroishi C, Tahirov TH. Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein. Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1846-54. Epub 2004, Sep 23. PMID:15388932 doi:10.1107/S0907444904019420
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