6ktq: Difference between revisions
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==Crystal structure of catalytic domain of homocitrate synthase from Sulfolobus acidocaldarius (SaHCS(dRAM)) in complex with alpha-ketoglutarate/Zn2+/CoA== | ==Crystal structure of catalytic domain of homocitrate synthase from Sulfolobus acidocaldarius (SaHCS(dRAM)) in complex with alpha-ketoglutarate/Zn2+/CoA== | ||
<StructureSection load='6ktq' size='340' side='right'caption='[[6ktq]]' scene=''> | <StructureSection load='6ktq' size='340' side='right'caption='[[6ktq]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KTQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KTQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ktq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulac Sulac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KTQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KTQ FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ktq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ktq OCA], [http://pdbe.org/6ktq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ktq RCSB], [http://www.ebi.ac.uk/pdbsum/6ktq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ktq ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Saci_1304 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330779 SULAC])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homocitrate_synthase Homocitrate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.14 2.3.3.14] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ktq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ktq OCA], [http://pdbe.org/6ktq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ktq RCSB], [http://www.ebi.ac.uk/pdbsum/6ktq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ktq ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/HOSA_SULAC HOSA_SULAC]] Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway. Does not display 2-isopropylmalate synthase and citramalate synthase activities since it cannot use 2-oxoisovalerate or pyruvate as substrate.<ref>PMID:31330039</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Homocitrate synthase (HCS) catalyzes the aldol condensation of alpha-ketoglutarate and acetyl coenzyme A to form homocitrate, which is the first committed step of lysine biosynthesis through the alpha-aminoadipate pathway in yeast, fungi, and some prokaryotes. We determined the crystal structure of a truncated form of HCS from a hyperthermophilic acidophilic archaeon, Sulfolobus acidocaldarius, which lacks the RAM (Regulation of amino acid metabolism) domain at the C terminus serving as the regulatory domain for the feedback inhibition by lysine, in complex with alpha-ketoglutarate, Mg(2+) , and CoA. This structure coupled with mutational analysis revealed that a subdomain, subdomain II, connecting the N-terminal catalytic domain and C-terminal RAM domain is involved in the recognition of acetyl-CoA. This is the first structural evidence of the function of subdomain II in the related enzyme family, which will lead to a better understanding of the catalytic mechanism of HCS. DATABASES: Structural data are available in the RCSB PDB database under the accession number 6KTQ. | |||
Involvement of subdomain II in the recognition of acetyl-CoA revealed by the crystal structure of homocitrate synthase from Sulfolobus acidocaldarius.,Suzuki T, Tomita T, Hirayama K, Suzuki M, Kuzuyama T, Nishiyama M FEBS J. 2020 Sep 8. doi: 10.1111/febs.15527. PMID:32897601<ref>PMID:32897601</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ktq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homocitrate synthase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kuzuyama T]] | [[Category: Sulac]] | ||
[[Category: Nishiyama M]] | [[Category: Kuzuyama, T]] | ||
[[Category: Suzuki T]] | [[Category: Nishiyama, M]] | ||
[[Category: Tomita T]] | [[Category: Suzuki, T]] | ||
[[Category: Tomita, T]] | |||
[[Category: Biosynthetic protein]] | |||
[[Category: Complex]] | |||
[[Category: Lyase]] | |||
[[Category: Sulfolobus acidocaldarius]] | |||
Revision as of 11:22, 23 September 2020
Crystal structure of catalytic domain of homocitrate synthase from Sulfolobus acidocaldarius (SaHCS(dRAM)) in complex with alpha-ketoglutarate/Zn2+/CoA
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