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==Structure of Azospirillum brasilense Glutamate Synthase in a4b3 oligomeric state== | |||
<StructureSection load='6s6t' size='340' side='right'caption='[[6s6t]], [[Resolution|resolution]] 4.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6s6t]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29145 Atcc 29145]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S6T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S6T FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gltB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192 ATCC 29145]), gltD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192 ATCC 29145])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_synthase_(NADPH) Glutamate synthase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.13 1.4.1.13] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6s6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s6t OCA], [http://pdbe.org/6s6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s6t RCSB], [http://www.ebi.ac.uk/pdbsum/6s6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s6t ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial NADPH-dependent glutamate synthase (GltS) is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of two L-Glu molecules from L-Gln and 2-oxo-glutarate. GltS functional unit hosts an alpha-subunit (alphaGltS) and a beta-subunit (betaGltS) that assemble in different alphabeta oligomers in solution. Here, we present the cryo-electron microscopy structures of Azospirillum brasilense GltS in four different oligomeric states (alpha4beta3, alpha4beta4, alpha6beta4 and alpha6beta6, in the 3.5- to 4.1-A resolution range). Our study provides a comprehensive GltS model that details the inter-protomeric assemblies and allows unequivocal location of the FAD cofactor and of two electron transfer [4Fe-4S](+1,+2) clusters within betaGltS. | |||
Cryo-EM Structures of Azospirillum brasilense Glutamate Synthase in Its Oligomeric Assemblies.,Swuec P, Chaves-Sanjuan A, Camilloni C, Vanoni MA, Bolognesi M J Mol Biol. 2019 Aug 29. pii: S0022-2836(19)30520-0. doi:, 10.1016/j.jmb.2019.08.011. PMID:31473159<ref>PMID:31473159</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6s6t" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Atcc 29145]] | |||
[[Category: Large Structures]] | |||
[[Category: Bolognesi, M]] | |||
[[Category: Chaves-Sanjuan, A]] | |||
[[Category: Complex]] | |||
[[Category: Flavoprotein]] | |||
[[Category: Glutamate synthesy]] | |||
[[Category: Oligomeric assembly]] | |||
Revision as of 11:49, 6 November 2019
Structure of Azospirillum brasilense Glutamate Synthase in a4b3 oligomeric stateStructure of Azospirillum brasilense Glutamate Synthase in a4b3 oligomeric state
Structural highlights
Publication Abstract from PubMedBacterial NADPH-dependent glutamate synthase (GltS) is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of two L-Glu molecules from L-Gln and 2-oxo-glutarate. GltS functional unit hosts an alpha-subunit (alphaGltS) and a beta-subunit (betaGltS) that assemble in different alphabeta oligomers in solution. Here, we present the cryo-electron microscopy structures of Azospirillum brasilense GltS in four different oligomeric states (alpha4beta3, alpha4beta4, alpha6beta4 and alpha6beta6, in the 3.5- to 4.1-A resolution range). Our study provides a comprehensive GltS model that details the inter-protomeric assemblies and allows unequivocal location of the FAD cofactor and of two electron transfer [4Fe-4S](+1,+2) clusters within betaGltS. Cryo-EM Structures of Azospirillum brasilense Glutamate Synthase in Its Oligomeric Assemblies.,Swuec P, Chaves-Sanjuan A, Camilloni C, Vanoni MA, Bolognesi M J Mol Biol. 2019 Aug 29. pii: S0022-2836(19)30520-0. doi:, 10.1016/j.jmb.2019.08.011. PMID:31473159[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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