1lm1: Difference between revisions

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-[[Image:1lm1.jpg|left|200px]]<br /><applet load="1lm1" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1lm1, resolution 2.80&Aring;" />
-'''Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme'''<br />
-==Overview==
+==Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme==
-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.
+<StructureSection load='1lm1' size='340' side='right'caption='[[1lm1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1lm1]] 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=1LM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LM1 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]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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=1lm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lm1 OCA], [https://pdbe.org/1lm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lm1 RCSB], [https://www.ebi.ac.uk/pdbsum/1lm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lm1 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/lm/1lm1_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=1lm1 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.
-==About this Structure==
+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>
-LM1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with ACT, FMN and F3S as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate_synthase_(ferredoxin) Glutamate synthase (ferredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.7.1 1.4.7.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LM1 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11967268 11967268]
+</div>
-[[Category: Glutamate synthase (ferredoxin)]]
+<div class="pdbe-citations 1lm1" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
-[[Category: Synechocystis sp.]]
-[[Category: Bossi, R.T.]]
-[[Category: Curti, B.]]
-[[Category: Ferrari, D.]]
-[[Category: Florencio, F.J.]]
-[[Category: Heuvel, R.H.van.Den.]]
-[[Category: Mattevi, A.]]
-[[Category: Ravasio, S.]]
-[[Category: Vanoni, M.A.]]
-[[Category: ACT]]
-[[Category: F3S]]
-[[Category: FMN]]
-[[Category: amidotransferase]]
-[[Category: channeling]]
-[[Category: glutamate synthase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:40:04 2007''
+==See Also==
+*[[Glutamate synthase|Glutamate synthase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Synechocystis sp. PCC 6803]]
+[[Category: Bossi RT]]
+[[Category: Curti B]]
+[[Category: Ferrari D]]
+[[Category: Florencio FJ]]
+[[Category: Mattevi A]]
+[[Category: Ravasio S]]
+[[Category: Vanoni MA]]
+[[Category: Van Den Heuvel RH]]