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Open data
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Basic information
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| Title | Alcohol Oxidase Mod1p from Ogataea methanolica | |||||||||
Map data | full | |||||||||
Sample |
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Keywords | ALCOHOL OXIDASE / OXIDOREDUCTASE MODIFIED FAD (A-FAD) / Mod1p / OXIDOREDUCTASE | |||||||||
| Function / homology | Function and homology informationmethane catabolic process / alcohol oxidase activity / alcohol oxidase / methanol metabolic process / peroxisomal matrix / flavin adenine dinucleotide binding Similarity search - Function | |||||||||
| Biological species | Ogataea methanolica (fungus) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 1.94 Å | |||||||||
Authors | Cai H-L / Shimada A / Hamaguchi T / Mizoguchi A / Yonekura K / Shimada M / Ebihara A / Tani K / Nakagawa T | |||||||||
| Funding support | Japan, 2 items
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Citation | Journal: Microb Biotechnol / Year: 2026Title: Cryo-EM Structures of Alcohol Oxidase Isozymes Reveal Structural Determinants of Cofactor Variation and Enzymatic Activity in Ogataea methanolica. Authors: Hao-Liang Cai / Atsuhiro Shimada / Tasuku Hamaguchi / Akira Mizoguchi / Koji Yonekura / Kyohei Tsuchiyama / Masaya Shimada / Akio Ebihara / Kazutoshi Tani / Tomoyuki Nakagawa / ![]() Abstract: Ogataea methanolica is a methylotrophic yeast that can produce diverse recombinant proteins using methanol as the sole carbon and energy source. Unlike most yeast species, which possess a single ...Ogataea methanolica is a methylotrophic yeast that can produce diverse recombinant proteins using methanol as the sole carbon and energy source. Unlike most yeast species, which possess a single alcohol oxidase, O. methanolica encodes two isoenzymes, Mod1p and Mod2p. This study examines the structural and functional differences between Mod1p and Mod2p homooctamers. Both enzymes were purified from MOD-disrupted strains and analysed using cryogenic electron microscopy, achieving resolutions of 1.9 and 2.7 Å for Mod1p and Mod2p, respectively. The two isozymes assemble as tetramers of dimers stabilized by extensive intersubunit interactions, largely mediated by protruding loop regions and C-terminal extensions. Despite overall structural similarities, Mod1p and Mod2p exhibit subtle differences in surface charge distribution and sequence composition within the FAD-binding domain. These variations correlate with distinct cofactor preferences, with Mod1p binding arabityl FAD and Mod2p binding canonical FAD. Thin-section electron microscopy further revealed that Mod1p and Mod2p form both homomeric and hybrid octamers that assemble into peroxisomal crystalloids essential for methanol metabolism. Collectively, our findings provide mechanistic insight into alcohol oxidase diversity in methylotrophic yeasts, advancing our understanding of methanol utilization and its applications in biotechnology. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_67739.map.gz | 229.3 MB | EMDB map data format | |
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| Header (meta data) | emd-67739-v30.xml emd-67739.xml | 18.9 KB 18.9 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_67739_fsc.xml | 14.4 KB | Display | FSC data file |
| Images | emd_67739.png | 107.5 KB | ||
| Filedesc metadata | emd-67739.cif.gz | 6.2 KB | ||
| Others | emd_67739_half_map_1.map.gz emd_67739_half_map_2.map.gz | 189.2 MB 188.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-67739 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-67739 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 21juMC ![]() 21jvC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_67739.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | full | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.823 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: odd
| File | emd_67739_half_map_1.map | ||||||||||||
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| Annotation | odd | ||||||||||||
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| Density Histograms |
-Half map: even
| File | emd_67739_half_map_2.map | ||||||||||||
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| Annotation | even | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Mod1p octamer in complex with a-FAD
| Entire | Name: Mod1p octamer in complex with a-FAD |
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| Components |
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-Supramolecule #1: Mod1p octamer in complex with a-FAD
| Supramolecule | Name: Mod1p octamer in complex with a-FAD / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Ogataea methanolica (fungus) |
-Macromolecule #1: alcohol oxidase
| Macromolecule | Name: alcohol oxidase / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO / EC number: alcohol oxidase |
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| Source (natural) | Organism: Ogataea methanolica (fungus) |
| Molecular weight | Theoretical: 74.011133 KDa |
| Sequence | String: MAIPDEFDII VVGGGSTGCA LAGRLGNLDE NVTVALIEGG ENNINNPWVY LPGVYPRNMR LDSKTATFYS SRPSPHLNGR RAIVPCANI LGGGSSINFL MYTRASASDY DDWESEGWTT DELLPLMKKI ETYQRPCNNR ELHGFDGPIK VSFGNYTYPN G QDFIRAAE ...String: MAIPDEFDII VVGGGSTGCA LAGRLGNLDE NVTVALIEGG ENNINNPWVY LPGVYPRNMR LDSKTATFYS SRPSPHLNGR RAIVPCANI LGGGSSINFL MYTRASASDY DDWESEGWTT DELLPLMKKI ETYQRPCNNR ELHGFDGPIK VSFGNYTYPN G QDFIRAAE SQGIPFVDDA EDLKCSHGAE HWLKWINRDL GRRSDSAHAY IHPTMRNKQN LFLITSTKCE KIIIENGVAT GI KTVPMKP TGSPKTQVAR TFKARKQIIV SCGTISSPLV LQRSGIGSAH KLRQVGIKPV VDLPGVGMNF QDHYCFFTPY HVK PDTPSF DDFVRGDKAV QKSAFDQWYA NKDGPLTTNG IEAGVKIRPT EEELATADDE FRAAYDDYFG NKPDKPLMHY SLIS GFFGD HTKIPNGKYM CMFHFLEYPF SRGFVHVVSP NPYDAPDFDP GFMNDPRDMW PMVWSYKKSR ETARRMDCFA GEVTS HHPH YPYDSPARAA DMDLETTKAY AGPDHFTANL YHGSWTVPIE KPTPKNAAHV TSNQVEKHRD IEYTKEDDAA IEDYIR EHT ETTWHCLGTC SMAPREGSKV VPTGGVVDSR LNVYGVEKLK VADLSICPDN VGCNTYSTAL LIGEKASTLV AEDLGYS GD ALKMTVPNFK LGTYEEAGLA RF UniProtKB: alcohol oxidase |
-Macromolecule #2: ARABINO-FLAVIN-ADENINE DINUCLEOTIDE
| Macromolecule | Name: ARABINO-FLAVIN-ADENINE DINUCLEOTIDE / type: ligand / ID: 2 / Number of copies: 8 / Formula: FAS |
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| Molecular weight | Theoretical: 785.55 Da |
| Chemical component information | ![]() ChemComp-FAS: |
-Macromolecule #3: water
| Macromolecule | Name: water / type: ligand / ID: 3 / Number of copies: 4384 / Formula: HOH |
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| Molecular weight | Theoretical: 18.015 Da |
| Chemical component information | ![]() ChemComp-HOH: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 6.5 mg/mL |
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| Buffer | pH: 7 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | JEOL CRYO ARM 300 |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 42.7 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.8000000000000003 µm / Nominal defocus min: 0.5 µm |
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About Yorodumi




Keywords
Ogataea methanolica (fungus)
Authors
Japan, 2 items
Citation



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Processing
FIELD EMISSION GUN

