|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3oyz' size='340' side='right'caption='[[3oyz]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='3oyz' size='340' side='right'caption='[[3oyz]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3oyz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloferax_volcanii Haloferax volcanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OYZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3oyz]] 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=3OYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OYZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</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]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3oyx|3oyx]], [[3pug|3pug]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Malate_synthase Malate synthase], with EC number [https://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=3oyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyz OCA], [https://pdbe.org/3oyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oyz RCSB], [https://www.ebi.ac.uk/pdbsum/3oyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oyz 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=3oyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyz OCA], [https://pdbe.org/3oyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oyz RCSB], [https://www.ebi.ac.uk/pdbsum/3oyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oyz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 27: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Haloferax volcanii]] | + | [[Category: Haloferax volcanii DS2]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Malate synthase]]
| + | [[Category: Bracken C]] |
| - | [[Category: Bracken, C]] | + | [[Category: Howard BR]] |
| - | [[Category: Howard, B R]] | + | [[Category: Lamlenn KK]] |
| - | [[Category: Lamlenn, K K]] | + | [[Category: Neighbor A]] |
| - | [[Category: Neighbor, A]] | + | [[Category: Schubert HL]] |
| - | [[Category: Schubert, H L]] | + | [[Category: Thomas G]] |
| - | [[Category: Thomas, G]] | + | [[Category: Whitby FG]] |
| - | [[Category: Whitby, F G]] | + | |
| - | [[Category: Tim barrel]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
3oyz is a 1 chain structure with sequence from Haloferax volcanii DS2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.95Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
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.[1] [2] [3]
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Serrano JA, Bonete MJ. Sequencing, phylogenetic and transcriptional analysis of the glyoxylate bypass operon (ace) in the halophilic archaeon Haloferax volcanii. Biochim Biophys Acta. 2001 Aug 30;1520(2):154-62. PMID:11513957
- ↑ Bracken CD, Neighbor AM, Lamlenn KK, Thomas GC, Schubert HL, Whitby FG, Howard BR. Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G. BMC Struct Biol. 2011 May 10;11(1):23. PMID:21569248 doi:10.1186/1472-6807-11-23
- ↑ Serrano JA, Camacho M, Bonete MJ. Operation of glyoxylate cycle in halophilic archaea: presence of malate synthase and isocitrate lyase in Haloferax volcanii. FEBS Lett. 1998 Aug 28;434(1-2):13-6. PMID:9738442
- ↑ Bracken CD, Neighbor AM, Lamlenn KK, Thomas GC, Schubert HL, Whitby FG, Howard BR. Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G. BMC Struct Biol. 2011 May 10;11(1):23. PMID:21569248 doi:10.1186/1472-6807-11-23
|
