1lm1

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[[Image:1lm1.jpg|left|200px]]
 
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==Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme==
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The line below this paragraph, containing "STRUCTURE_1lm1", creates the "Structure Box" on the page.
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<StructureSection load='1lm1' size='340' side='right'caption='[[1lm1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_1lm1| PDB=1lm1 | SCENE= }}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLTS_SYNY3 GLTS_SYNY3]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/1lm1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme'''
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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>
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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1LM1 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=1LM1 OCA].
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</div>
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<div class="pdbe-citations 1lm1" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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]
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*[[Glutamate synthase|Glutamate synthase]]
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[[Category: Single protein]]
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== References ==
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[[Category: Synechocystis sp.]]
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<references/>
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[[Category: Bossi, R T.]]
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__TOC__
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[[Category: Curti, B.]]
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</StructureSection>
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[[Category: Ferrari, D.]]
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[[Category: Large Structures]]
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[[Category: Florencio, F J.]]
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[[Category: Synechocystis sp. PCC 6803]]
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[[Category: Heuvel, R H.van Den.]]
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[[Category: Bossi RT]]
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[[Category: Mattevi, A.]]
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[[Category: Curti B]]
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[[Category: Ravasio, S.]]
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[[Category: Ferrari D]]
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[[Category: Vanoni, M A.]]
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[[Category: Florencio FJ]]
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[[Category: Amidotransferase]]
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[[Category: Mattevi A]]
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[[Category: Channeling]]
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[[Category: Ravasio S]]
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[[Category: Glutamate synthase]]
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[[Category: Vanoni MA]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:03:05 2008''
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[[Category: Van Den Heuvel RH]]

Current revision

Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme

PDB ID 1lm1

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