1jh0: Difference between revisions

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-{{Seed}}
-[[Image:1jh0.png|left|200px]]
-<!--
+==Photosynthetic Reaction Center Mutant With Glu L 205 Replaced to Leu==
-The line below this paragraph, containing "STRUCTURE_1jh0", creates the "Structure Box" on the page.
+<StructureSection load='1jh0' size='340' side='right'caption='[[1jh0]], [[Resolution|resolution]] 3.50&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'>[[1jh0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JH0 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]] 3.5&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SPO:SPHEROIDENE'>SPO</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></td></tr>
-{{STRUCTURE_1jh0|  PDB=1jh0  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jh0 OCA], [https://pdbe.org/1jh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jh0 RCSB], [https://www.ebi.ac.uk/pdbsum/1jh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jh0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RCEL_CERSP RCEL_CERSP] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
+== 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/jh/1jh0_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=1jh0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The role of contact interactions in the crystallization of membrane proteins was assessed by mutation of amino-acid residues on the surface of the reaction center from Rhodobacter sphaeroides. Five single-site mutants were constructed, with changes in contact regions found in the trigonal and tetragonal forms but not the orthorhombic form. Crystallization trials for the tetragonal form yielded either no crystals or crystals with an altered morphology, whereas crystals grew in the other two forms, indicating that these interactions are essential for the stability of the tetragonal crystals. Changes in the structures determined by X-ray diffraction of trigonal crystals for each mutant were related to the quality of the diffraction. Significant differences in the resolution limit of the crystals were associated with the loss of specific interactions between neighboring proteins. The results suggest that the contact regions are crucial for obtaining highly ordered crystals of membrane proteins.
-===Photosynthetic Reaction Center Mutant With Glu L 205 Replaced to Leu===
+Individual interactions influence the crystalline order for membrane proteins.,Camara-Artigas A, Magee CL, Williams JC, Allen JP Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1281-6. Epub 2001, Aug 23. PMID:11526320<ref>PMID:11526320</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11526320}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1jh0" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11526320 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11526320}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Cereibacter sphaeroides]]
-JH0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JH0 OCA].
+[[Category: Large Structures]]
+[[Category: Allen JP]]
-==Reference==
+[[Category: Camara-Artigas A]]
-Individual interactions influence the crystalline order for membrane proteins., Camara-Artigas A, Magee CL, Williams JC, Allen JP, Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1281-6. Epub 2001, Aug 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11526320 11526320]
+[[Category: Magee CL]]
-[[Category: Protein complex]]
+[[Category: Williams JC]]
-[[Category: Rhodobacter sphaeroides]]
-[[Category: Allen, J P.]]
-[[Category: Camara-Artigas, A.]]
-[[Category: Magee, C L.]]
-[[Category: Williams, J C.]]
-[[Category: Alpha helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 20:13:55 2008''