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| | ==Haloferax volcanii Malate Synthase Lead(II) complex== | | ==Haloferax volcanii Malate Synthase Lead(II) complex== |
| - | <StructureSection load='5tao' size='340' side='right' caption='[[5tao]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5tao' size='340' side='right'caption='[[5tao]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tao]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TAO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tao]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloferax_volcanii_DS2 Haloferax volcanii DS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TAO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLV:GLYOXYLIC+ACID'>GLV</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3oyz|3oyz]], [[3pug|3pug]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLV:GLYOXYLIC+ACID'>GLV</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_synthase Malate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.9 2.3.3.9] </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=5tao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tao OCA], [https://pdbe.org/5tao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tao RCSB], [https://www.ebi.ac.uk/pdbsum/5tao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tao ProSAT]</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=5tao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tao OCA], [http://pdbe.org/5tao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tao RCSB], [http://www.ebi.ac.uk/pdbsum/5tao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tao ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACEB_HALVD ACEB_HALVD]] Involved in the glyoxylate cycle which synthesizes precursors for carbohydrates from C2 compounds such as acetate. Catalyzes the Claisen condensation between acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form the malyl-CoA intermediate that is subsequently hydrolyzed to produce malate and CoA.<ref>PMID:11513957</ref> <ref>PMID:21569248</ref> <ref>PMID:9738442</ref> | + | [https://www.uniprot.org/uniprot/ACEB_HALVD ACEB_HALVD] Involved in the glyoxylate cycle which synthesizes precursors for carbohydrates from C2 compounds such as acetate. Catalyzes the Claisen condensation between acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form the malyl-CoA intermediate that is subsequently hydrolyzed to produce malate and CoA.<ref>PMID:11513957</ref> <ref>PMID:21569248</ref> <ref>PMID:9738442</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | ABSTRACT: BACKGROUND: Malate synthase, one of the two enzymes unique to the glyoxylate cycle, is found in all three domains of life, and is crucial to the utilization of two-carbon compounds for net biosynthetic pathways such as gluconeogenesis. In addition to the main isoforms A and G, so named because of their differential expression in E. coli grown on either acetate or glycolate respectively, a third distinct isoform has been identified. These three isoforms differ considerably in size and sequence conservation. The A isoform (MSA) comprises ~530 residues, the G isoform (MSG) is ~730 residues, and this third isoform (MSH- halophilic) is ~430 residues in length. Both isoforms A and G have been structurally characterized in detail, but no structures have been reported for the H isoform which has been found thus far only in members of the halophilic Archaea. RESULTS: We have solved the structure of a malate synthase H (MSH) isoform member from Haloferax volcanii in complex with glyoxylate at 2.51 angstrom resolution, and also as a ternary complex with acetyl-coenzyme A and pyruvate at 1.95 angstroms. Like the A and G isoforms, MSH is based on a beta8/alpha8 (TIM) barrel. Unlike previously solved malate synthase structures which are all monomeric, this enzyme is found in the native state as a trimer/hexamer equilibrium. Compared to isoforms A and G, MSH displays deletion of an N-terminal domain and a smaller deletion at the C-terminus. The MSH active site is closely superimposable with those of MSA and MSG, with the ternary complex indicating a nucleophilic attack on pyruvate by the enolate intermediate of acetyl-coenzyme A. CONCLUSIONS: The reported structures of MSH from Haloferax volcanii allow a detailed analysis and comparison with previously solved structures of isoforms A and G. These structural comparisons provide insight into evolutionary relationships among these isoforms, and also indicate that despite the size and sequence variation, and the truncated C-terminal domain of the H isoform, the catalytic mechanism is conserved. Sequence analysis in light of the structure indicates that additional members of isoform H likely exist in the databases but have been misannotated.
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| - | Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G.,Bracken CD, Neighbor AM, Lamlenn KK, Thomas GC, Schubert HL, Whitby FG, Howard BR BMC Struct Biol. 2011 May 10;11(1):23. PMID:21569248<ref>PMID:21569248</ref>
| + | ==See Also== |
| - | | + | *[[Malate synthase 3D structures|Malate synthase 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5tao" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Malate synthase]] | + | [[Category: Haloferax volcanii DS2]] |
| - | [[Category: Adams, M J]] | + | [[Category: Large Structures]] |
| - | [[Category: Howard, B R]] | + | [[Category: Adams MJ]] |
| - | [[Category: Transferase]] | + | [[Category: Howard BR]] |
