1us4: Difference between revisions

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-[[Image:1us4.jpg|left|200px]]<br /><applet load="1us4" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1us4, resolution 1.75&Aring;" />
-'''PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE'''<br />
-==Overview==
+==PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE==
-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.
+<StructureSection load='1us4' size='340' side='right'caption='[[1us4]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+== Structural highlights ==
+<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='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>
+<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='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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/P83817_THETH P83817_THETH]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/us/1us4_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </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/main_output.php?pdb_ID=1us4 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==About this Structure==
+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<ref>PMID:15388932</ref>
-US4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=GLU:'>GLU</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=EGL:GLU+Binding+Site+For+Chain+A'>EGL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1US4 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15388932 15388932]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 1us4" style="background-color:#fffaf0;"></div>
-[[Category: Thermus thermophilus]]
+== References ==
-[[Category: Inagaki, E.]]
+<references/>
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+__TOC__
-[[Category: Tahirov, T.H.]]
+</StructureSection>
-[[Category: Takahashi, H.]]
+[[Category: Large Structures]]
-[[Category: EDO]]
+[[Category: Thermus thermophilus HB8]]
-[[Category: GLU]]
+[[Category: Inagaki E]]
-[[Category: glur0]]
+[[Category: Tahirov TH]]
-[[Category: glutamate receptor]]
+[[Category: Takahashi H]]
-[[Category: l-glutamate]]
-[[Category: membrane protein]]
-[[Category: riken structural genomics/proteomics initiative]]
-[[Category: rsgi]]
-[[Category: structural genomics]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:04:19 2008''