2q2c: Difference between revisions

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-[[Image:2q2c.jpg|left|200px]]
-<!--
+==Crystal structures of the arginine-, lysine-, histidine-binding protein ArtJ from the thermophilic bacterium Geobacillus stearothermophilus==
-The line below this paragraph, containing "STRUCTURE_2q2c", creates the "Structure Box" on the page.
+<StructureSection load='2q2c' size='340' side='right'caption='[[2q2c]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2q2c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q2C FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_2q2c|  PDB=2q2c  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q2c OCA], [https://pdbe.org/2q2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q2c RCSB], [https://www.ebi.ac.uk/pdbsum/2q2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q2c ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/D0VWX8_GEOSE D0VWX8_GEOSE]
+== 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/q2/2q2c_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=2q2c ConSurf].
+<div style="clear:both"></div>
-'''Crystal structures of the arginine-, lysine-, histidine-binding protein ArtJ from the thermophilic bacterium Geobacillus stearothermophilus'''
+==See Also==
+*[[ABC transporter 3D structures|ABC transporter 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-ArtJ is the substrate-binding component (receptor) of the ATP-binding cassette (ABC) transport system ArtJ-(MP)(2) from the thermophilic bacterium Geobacillus stearothermophilus that is specific for arginine, lysine, and histidine. The highest affinity is found for arginine (K(d)=0.039(+/-0.014) microM), while the affinities for lysine and histidine are about tenfold lower. We have determined the X-ray structures of ArtJ liganded with each of these substrates at resolutions of 1.79 A (arginine), 1.79 A (lysine), and 2.35 A (histidine), respectively. As found for other solute receptors, the polypeptide chain is folded into two distinct domains (lobes) connected by a hinge. The interface between the lobes forms the substrate-binding pocket whose geometry is well preserved in all three ArtJ/amino acid complexes. Structure-derived mutational analyses indicated the crucial role of a region in the carboxy-terminal lobe of ArtJ in contacting the transport pore Art(MP)(2) and revealed the functional importance of Gln132 and Trp68. While variant Gln132Leu exhibited lower binding affinity for arginine but no binding of lysine and histidine, the variant Trp68Leu had lost binding activity for all three substrates. The results are discussed in comparison with known structures of homologous proteins from mesophilic bacteria.
+[[Category: Geobacillus stearothermophilus]]
+[[Category: Large Structures]]
-==About this Structure==
+[[Category: Eckey V]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q2C OCA].
+[[Category: Saenger W]]
+[[Category: Scheffel F]]
-==Reference==
+[[Category: Schneider E]]
-Crystal structures and mutational analysis of the arginine-, lysine-, histidine-binding protein ArtJ from Geobacillus stearothermophilus. Implications for interactions of ArtJ with its cognate ATP-binding cassette transporter, Art(MP)2., Vahedi-Faridi A, Eckey V, Scheffel F, Alings C, Landmesser H, Schneider E, Saenger W, J Mol Biol. 2008 Jan 11;375(2):448-59. Epub 2007 Oct 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18022195 18022195]
+[[Category: Vahedi-Faridi A]]
-[[Category: Eckey, V.]]
-[[Category: Saenger, W.]]
-[[Category: Scheffel, F.]]
-[[Category: Schneider, E.]]
-[[Category: Vahedi-Faridi, A.]]
-[[Category: Abc transport system]]
-[[Category: Basic amino acid binding protein]]
-[[Category: Thermophilic bacterium]]
-[[Category: Transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 14:12:01 2008''