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- SASDAF4: DmMfe2 (Peroxisomal multifunctional enzyme type 2) -

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Basic information

Entry
Database: SASBDB / ID: SASDAF4
SampleDmMfe2
  • Peroxisomal multifunctional enzyme type 2 (protein), DmMfe2, Drosophila melanogaster
Function / homology
Function and homology information


Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / alpha-linolenic acid (ALA) metabolism / Beta-oxidation of pristanoyl-CoA / Beta-oxidation of very long chain fatty acids / Peroxisomal protein import / (3R)-hydroxyacyl-CoA dehydrogenase (NAD+) activity / : / enoyl-CoA hydratase 2 / 3-hydroxyacyl-CoA dehydratase activity / fatty acid beta-oxidation using acyl-CoA oxidase ...Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / alpha-linolenic acid (ALA) metabolism / Beta-oxidation of pristanoyl-CoA / Beta-oxidation of very long chain fatty acids / Peroxisomal protein import / (3R)-hydroxyacyl-CoA dehydrogenase (NAD+) activity / : / enoyl-CoA hydratase 2 / 3-hydroxyacyl-CoA dehydratase activity / fatty acid beta-oxidation using acyl-CoA oxidase / 17-beta-hydroxysteroid dehydrogenase (NAD+) activity / 3-hydroxyacyl-CoA dehydrogenase activity / estradiol 17-beta-dehydrogenase [NAD(P)+] activity / enoyl-CoA hydratase activity / fatty acid beta-oxidation / peroxisome / protein homodimerization activity
Similarity search - Function
MaoC-like dehydratase domain / MaoC like domain / short chain dehydrogenase / PKS_KR / HotDog domain superfamily / Short-chain dehydrogenase/reductase, conserved site / Short-chain dehydrogenases/reductases family signature. / Short-chain dehydrogenase/reductase SDR / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
Peroxisomal multifunctional enzyme type 2
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
CitationJournal: FEBS Lett / Year: 2013
Title: Quaternary structure of human, Drosophila melanogaster and Caenorhabditis elegans MFE-2 in solution from synchrotron small-angle X-ray scattering.
Authors: Maija L Mehtälä / Tatu J K Haataja / Clément E Blanchet / J Kalervo Hiltunen / Dmitri I Svergun / Tuomo Glumoff /
Abstract: Multifunctional enzyme type 2 (MFE-2) forms part of the fatty acid β-oxidation pathway in peroxisomes. MFE-2s from various species reveal proteins with structurally homologous functional domains ...Multifunctional enzyme type 2 (MFE-2) forms part of the fatty acid β-oxidation pathway in peroxisomes. MFE-2s from various species reveal proteins with structurally homologous functional domains assembled in different compilations. Crystal structures of all domain types are known. SAXS data from human, fruit fly and Caenorhabditiselegans MFE-2s and their constituent domains were collected, and both ab initio and rigid body models constructed. Location of the putative substrate binding helper domain SCP-2L (sterol carrier protein 2-like), which is not part of MFE-2 protein in every species and not seen as part of any previous MFE-2 structures, was determined. The obtained models of human and C. elegans MFE-2 lend a direct structural support to the idea of the biological role of SCP-2L.
Contact author
  • Clement Blanchet (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

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Models

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Sample

SampleName: DmMfe2 / Specimen concentration: 7.60-11.20
BufferName: Sodium Phosphate / Concentration: 20.00 mM / pH: 7.5 / Composition: 200 NaCl 5% (v/v) Glycerol 1mM Na2EDTA 1mMNaN3
Entity #148Name: DmMfe2 / Type: protein / Description: Peroxisomal multifunctional enzyme type 2 / Formula weight: 64 / Num. of mol.: 2 / Source: Drosophila melanogaster / References: UniProt: Q9VXJ0
Sequence: MSSSDGKLRY DGRVAVVTGA GAGLGREYAL LFAERGAKVV VNDLGGTHSG DGASQRAADI VVDEIRKAGG EAVADYNSVI DGAKVIETAI KAFGRVDILV NNAGILRDRS LVKTSEQDWN LVNDVHLKGS FKCTQAAFPY MKKQNYGRII MTSSNSGIYG NFGQVNYTAA ...Sequence:
MSSSDGKLRY DGRVAVVTGA GAGLGREYAL LFAERGAKVV VNDLGGTHSG DGASQRAADI VVDEIRKAGG EAVADYNSVI DGAKVIETAI KAFGRVDILV NNAGILRDRS LVKTSEQDWN LVNDVHLKGS FKCTQAAFPY MKKQNYGRII MTSSNSGIYG NFGQVNYTAA KMGLIGLANT VAIEGARNNV LCNVIVPTAA SRMTEGILPD ILFNELKPKL IAPVVAYLCH ESCEDNGSYI ESAAGWATKL HMVRGKGAVL RPSLDDPVTI EYVKDVWSNV TDMSKAKHLG AIAEASGTLL EVLEKLKEGG GDAIEDAFEF NSKELITYAL GIGASVKNAK DMRFLYENDA DFAAIPTFFV LPGLLLQMST DKLLSKALPN SQVDFSNILH GEQYLEIVDD LPTSGTLLTN GKVFDVMDKG SGAVVVTNSE SFDESGRLLV RNQSTTFIVG AGKFGGKKDP IAGVVPLQPA PNRQPDATVQ YTTSEDQAAL YRLSGDKNPL HIDPQMALLA GFKTPILHGL CTLGFSVRAV LAQFADNNPA LFKAVKVRFS GPVIPGQTLR VDLWKQGTRI NFRTVVVETG KEVISGAYVD LKSSQAKL

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Experimental information

BeamInstrument name: DORIS III X33 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron
DetectorName: MAR 345 Image Plate
Scan
Title: DmMFE-2 / Measurement date: Jun 12, 2010 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 30 sec. / Number of frames: 4 / Unit: 1/nm /
MinMax
Q0.1077 6.3425
ResultType of curve: merged / Standard: BSA /
ExperimentalStandardEstimated
MW80 kDa80 kDa-
Volume--200

GuinierP(R)
Forward scattering, I091.2 -
Radius of gyration, Rg3.6 nm3.6 nm

MinMax
D-12
Guinier point11 94

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