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| | <StructureSection load='6ktq' size='340' side='right'caption='[[6ktq]], [[Resolution|resolution]] 1.98Å' scene=''> | | <StructureSection load='6ktq' size='340' side='right'caption='[[6ktq]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <table><tr><td colspan='2'>[[6ktq]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=6KTQ FirstGlance]. <br> |
| | </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> | | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Saci_1304 ([https://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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Homocitrate_synthase Homocitrate synthase], with EC number [https://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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ktq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ktq OCA], [https://pdbe.org/6ktq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ktq RCSB], [https://www.ebi.ac.uk/pdbsum/6ktq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ktq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [[https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Structural highlights
6ktq is a 2 chain structure with sequence from Sulac. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , |
| Gene: | Saci_1304 (SULAC) |
| Activity: | Homocitrate synthase, with EC number 2.3.3.14 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Suzuki T, Akiyama N, Yoshida A, Tomita T, Lassak K, Haurat MF, Okada T, Takahashi K, Albers SV, Kuzuyama T, Nishiyama M. Biochemical characterization of archaeal homocitrate synthase from Sulfolobus acidocaldarius. FEBS Lett. 2020 Jan;594(1):126-134. doi: 10.1002/1873-3468.13550. Epub 2019 Aug, 1. PMID:31330039 doi:http://dx.doi.org/10.1002/1873-3468.13550
- ↑ Suzuki T, Tomita T, Hirayama K, Suzuki M, Kuzuyama T, Nishiyama M. Involvement of subdomain II in the recognition of acetyl-CoA revealed by the crystal structure of homocitrate synthase from Sulfolobus acidocaldarius. FEBS J. 2020 Sep 8. doi: 10.1111/febs.15527. PMID:32897601 doi:http://dx.doi.org/10.1111/febs.15527
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