1llz: Difference between revisions

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-[[Image:1llz.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1llz", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1llz|  PDB=1llz  |  SCENE=  }}
-'''Structural studies on the synchronization of catalytic centers in glutamate synthase: reduced enzyme'''
+==Structural studies on the synchronization of catalytic centers in glutamate synthase: reduced enzyme==
+<StructureSection load='1llz' size='340' side='right'caption='[[1llz]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1llz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLZ 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]] 3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=1llz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llz OCA], [https://pdbe.org/1llz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1llz RCSB], [https://www.ebi.ac.uk/pdbsum/1llz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1llz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GLTS_SYNY3 GLTS_SYNY3]
+== 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/ll/1llz_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=1llz ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The complex iron-sulfur flavoprotein glutamate synthase (GltS) plays a prominent role in ammonia assimilation in bacteria, yeasts, and plants. GltS catalyzes the formation of two molecules of l-glutamate from 2-oxoglutarate and l-glutamine via intramolecular channeling of ammonia. GltS has the impressive ability of synchronizing its distinct catalytic centers to avoid wasteful consumption of l-glutamine. We have determined the crystal structure of the ferredoxin-dependent GltS in several ligation and redox states. The structures reveal the crucial elements in the synchronization between the glutaminase site and the 2-iminoglutarate reduction site. The structural data combined with the catalytic properties of GltS indicate that binding of ferredoxin and 2-oxoglutarate to the FMN-binding domain of GltS induce a conformational change in the loop connecting the two catalytic centers. The rearrangement induces a shift in the catalytic elements of the amidotransferase domain, such that it becomes activated. This machinery, over a distance of more than 30 A, controls the ability of the enzyme to bind and hydrolyze the ammonia-donating substrate l-glutamine.
-==Overview==
+Structural studies on the synchronization of catalytic centers in glutamate synthase.,van den Heuvel RH, Ferrari D, Bossi RT, Ravasio S, Curti B, Vanoni MA, Florencio FJ, Mattevi A J Biol Chem. 2002 Jul 5;277(27):24579-83. Epub 2002 Apr 19. PMID:11967268<ref>PMID:11967268</ref>
-The complex iron-sulfur flavoprotein glutamate synthase (GltS) plays a prominent role in ammonia assimilation in bacteria, yeasts, and plants. GltS catalyzes the formation of two molecules of l-glutamate from 2-oxoglutarate and l-glutamine via intramolecular channeling of ammonia. GltS has the impressive ability of synchronizing its distinct catalytic centers to avoid wasteful consumption of l-glutamine. We have determined the crystal structure of the ferredoxin-dependent GltS in several ligation and redox states. The structures reveal the crucial elements in the synchronization between the glutaminase site and the 2-iminoglutarate reduction site. The structural data combined with the catalytic properties of GltS indicate that binding of ferredoxin and 2-oxoglutarate to the FMN-binding domain of GltS induce a conformational change in the loop connecting the two catalytic centers. The rearrangement induces a shift in the catalytic elements of the amidotransferase domain, such that it becomes activated. This machinery, over a distance of more than 30 A, controls the ability of the enzyme to bind and hydrolyze the ammonia-donating substrate l-glutamine.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-LLZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLZ OCA].
+</div>
+<div class="pdbe-citations 1llz" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structural studies on the synchronization of catalytic centers in glutamate synthase., van den Heuvel RH, Ferrari D, Bossi RT, Ravasio S, Curti B, Vanoni MA, Florencio FJ, Mattevi A, J Biol Chem. 2002 Jul 5;277(27):24579-83. Epub 2002 Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11967268 11967268]
+*[[Glutamate synthase|Glutamate synthase]]
-[[Category: Single protein]]
+== References ==
-[[Category: Synechocystis sp.]]
+<references/>
-[[Category: Bossi, R T.]]
+__TOC__
-[[Category: Curti, B.]]
+</StructureSection>
-[[Category: Ferrari, D.]]
+[[Category: Large Structures]]
-[[Category: Florencio, F J.]]
+[[Category: Synechocystis sp. PCC 6803]]
-[[Category: Heuvel, R H.van den.]]
+[[Category: Bossi RT]]
-[[Category: Mattevi, A.]]
+[[Category: Curti B]]
-[[Category: Ravasio, S.]]
+[[Category: Ferrari D]]
-[[Category: Vanoni, M A.]]
+[[Category: Florencio FJ]]
-[[Category: Amidotransferase]]
+[[Category: Mattevi A]]
-[[Category: Channeling]]
+[[Category: Ravasio S]]
-[[Category: Glutamate synthase]]
+[[Category: Vanoni MA]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:02:52 2008''
+[[Category: Van den Heuvel RH]]