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| | <StructureSection load='5hsa' size='340' side='right'caption='[[5hsa]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='5hsa' size='340' side='right'caption='[[5hsa]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hsa]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Kompc Kompc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HSA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HSA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hsa]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataella_phaffii_CBS_7435 Komagataella phaffii CBS 7435]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HSA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAS:ARABINO-FLAVIN-ADENINE+DINUCLEOTIDE'>FAS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.35Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AOX1, PP7435_Chr4-0130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=981350 KOMPC])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAS:ARABINO-FLAVIN-ADENINE+DINUCLEOTIDE'>FAS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_oxidase Alcohol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.13 1.1.3.13] </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=5hsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hsa OCA], [https://pdbe.org/5hsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hsa RCSB], [https://www.ebi.ac.uk/pdbsum/5hsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hsa ProSAT]</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=5hsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hsa OCA], [http://pdbe.org/5hsa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hsa RCSB], [http://www.ebi.ac.uk/pdbsum/5hsa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hsa ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALOX1_KOMPC ALOX1_KOMPC]] Major isoform of alcohol oxidase, which catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts.<ref>PMID:2657390</ref> <ref>PMID:9396748</ref> | + | [https://www.uniprot.org/uniprot/ALOX1_KOMPC ALOX1_KOMPC] Major isoform of alcohol oxidase, which catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts.<ref>PMID:2657390</ref> <ref>PMID:9396748</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alcohol oxidase]] | + | [[Category: Komagataella phaffii CBS 7435]] |
| - | [[Category: Kompc]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Feussner, I]] | + | [[Category: Feussner I]] |
| - | [[Category: Ficner, R]] | + | [[Category: Ficner R]] |
| - | [[Category: Koch, C]] | + | [[Category: Koch C]] |
| - | [[Category: Neumann, P]] | + | [[Category: Neumann P]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
5hsa is a 8 chain structure with sequence from Komagataella phaffii CBS 7435. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.35Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
ALOX1_KOMPC Major isoform of alcohol oxidase, which catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts.[1] [2]
Publication Abstract from PubMed
FAD-dependent alcohol oxidases (AOX) are key enzymes of methylotrophic organisms that can utilize lower primary alcohols as sole source of carbon and energy. Here we report the crystal structure analysis of the methanol oxidase AOX1 from Pichia pastoris. The crystallographic phase problem was solved by means of Molecular Replacement in combination with initial structure rebuilding using Rosetta model completion and relaxation against an averaged electron density map. The subunit arrangement of the homo-octameric AOX1 differs from that of octameric vanillyl alcohol oxidase and other dimeric or tetrameric alcohol oxidases, due to the insertion of two large protruding loop regions and an additional C-terminal extension in AOX1. In comparison to other alcohol oxidases, the active site cavity of AOX1 is significantly reduced in size, which could explain the observed preference for methanol as substrate. All AOX1 subunits of the structure reported here harbor a modified flavin adenine dinucleotide, which contains an arabityl chain instead of a ribityl chain attached to the isoalloxazine ring.
Crystal Structure of Alcohol Oxidase from Pichia pastoris.,Koch C, Neumann P, Valerius O, Feussner I, Ficner R PLoS One. 2016 Feb 23;11(2):e0149846. doi: 10.1371/journal.pone.0149846., eCollection 2016. PMID:26905908[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cregg JM, Madden KR, Barringer KJ, Thill GP, Stillman CA. Functional characterization of the two alcohol oxidase genes from the yeast Pichia pastoris. Mol Cell Biol. 1989 Mar;9(3):1316-23. PMID:2657390
- ↑ Waterham HR, Russell KA, Vries Y, Cregg JM. Peroxisomal targeting, import, and assembly of alcohol oxidase in Pichia pastoris. J Cell Biol. 1997 Dec 15;139(6):1419-31. PMID:9396748
- ↑ Koch C, Neumann P, Valerius O, Feussner I, Ficner R. Crystal Structure of Alcohol Oxidase from Pichia pastoris. PLoS One. 2016 Feb 23;11(2):e0149846. doi: 10.1371/journal.pone.0149846., eCollection 2016. PMID:26905908 doi:http://dx.doi.org/10.1371/journal.pone.0149846
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