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Yorodumi- SASDEL9: Escherichia coli aerobic fatty acid beta-oxidation trifunctional ... -
+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDEL9 |
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Sample | Escherichia coli aerobic fatty acid beta-oxidation trifunctional enzyme complex
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Function / homology | Function and homology information fatty acid beta-oxidation multienzyme complex / 3-hydroxybutyryl-CoA epimerase / 3-hydroxybutyryl-CoA epimerase activity / acetyl-CoA C-acyltransferase / Delta3-Delta2-enoyl-CoA isomerase / delta(3)-delta(2)-enoyl-CoA isomerase activity / acetyl-CoA C-acyltransferase activity / long-chain-3-hydroxyacyl-CoA dehydrogenase activity / 3-hydroxyacyl-CoA dehydrogenase / enoyl-CoA hydratase ...fatty acid beta-oxidation multienzyme complex / 3-hydroxybutyryl-CoA epimerase / 3-hydroxybutyryl-CoA epimerase activity / acetyl-CoA C-acyltransferase / Delta3-Delta2-enoyl-CoA isomerase / delta(3)-delta(2)-enoyl-CoA isomerase activity / acetyl-CoA C-acyltransferase activity / long-chain-3-hydroxyacyl-CoA dehydrogenase activity / 3-hydroxyacyl-CoA dehydrogenase / enoyl-CoA hydratase / phenylacetate catabolic process / 3-hydroxyacyl-CoA dehydrogenase activity / enoyl-CoA hydratase activity / fatty acid beta-oxidation / NAD+ binding / cytoplasm Similarity search - Function |
Biological species | Escherichia coli (strain K12) (bacteria) |
Citation | Journal: Biochem J / Year: 2019 Title: Complementary substrate specificity and distinct quaternary assembly of the aerobic and anaerobic β-oxidation trifunctional enzyme complexes. Authors: Shiv K Sah-Teli / Mikko J Hynönen / Werner Schmitz / James A Geraets / Jani Seitsonen / Jan Skov Pedersen / Sarah J Butcher / Rik K Wierenga / Rajaram Venkatesan / Abstract: The trifunctional enzyme (TFE) catalyzes the last three steps of the fatty acid β-oxidation cycle. Two TFEs are present in , EcTFE and anEcTFE. EcTFE is expressed only under aerobic conditions, ...The trifunctional enzyme (TFE) catalyzes the last three steps of the fatty acid β-oxidation cycle. Two TFEs are present in , EcTFE and anEcTFE. EcTFE is expressed only under aerobic conditions, whereas anEcTFE is expressed also under anaerobic conditions, with nitrate or fumarate as the ultimate electron acceptor. The anEcTFE subunits have higher sequence identity with the human mitochondrial TFE (HsTFE) than with the soluble EcTFE. Like HsTFE, here it is found that anEcTFE is a membrane-bound complex. Systematic enzyme kinetic studies show that anEcTFE has a preference for medium- and long-chain enoyl-CoAs, similar to HsTFE, whereas EcTFE prefers short chain enoyl-CoA substrates. The biophysical characterization of anEcTFE and EcTFE shows that EcTFE is heterotetrameric, whereas anEcTFE is purified as a complex of two heterotetrameric units, like HsTFE. The tetrameric assembly of anEcTFE resembles the HsTFE tetramer, although the arrangement of the two anEcTFE tetramers in the octamer is different from the HsTFE octamer. These studies demonstrate that EcTFE and anEcTFE have complementary substrate specificities, allowing for complete degradation of long-chain enoyl-CoAs under aerobic conditions. The new data agree with the notion that anEcTFE and HsTFE are evolutionary closely related, whereas EcTFE belongs to a separate subfamily. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDEL9 |
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-Related structure data
Related structure data | C: citing same article (ref.) |
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Similar structure data |
-External links
Related items in Molecule of the Month |
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-Models
Model #2747 | Type: dummy / Radius of dummy atoms: 5.80 A / Symmetry: p1 / Chi-square value: 1.029 / P-value: 0.936796 Search similar-shape structures of this assembly by Omokage search (details) |
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Model #2748 | Type: atomic Comment: subunits and complex were modeled using swissmodel and coot respectively using 1wdm.pdb as referenc Chi-square value: 1.357 / P-value: 0.000001 Search similar-shape structures of this assembly by Omokage search (details) |
-Sample
Sample | Name: Escherichia coli aerobic fatty acid beta-oxidation trifunctional enzyme complex Specimen concentration: 6.2 mg/ml / Entity id: 1432 / 1433 / 1434 |
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Buffer | Name: 20 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), 120 mM KCl, 2.5 mM DTT pH: 7.2 |
Entity #1432 | Name: EcTFE-alpha / Type: protein / Description: Fatty acid oxidation complex subunit alpha / Formula weight: 81.206 / Num. of mol.: 1 / Source: Escherichia coli (strain K12) / References: UniProt: P21177 Sequence: MGSSHHHHHH SQDPMLYKGD TLYLDWLEDG IAELVFDAPG SVNKLDTATV ASLGEAIGVL EQQSDLKGLL LRSNKAAFIV GADITEFLSL FLVPEEQLSQ WLHFANSVFN RLEDLPVPTI AAVNGYALGG GCECVLATDY RLATPDLRIG LPETKLGIMP GFGGSVRMPR ...Sequence: MGSSHHHHHH SQDPMLYKGD TLYLDWLEDG IAELVFDAPG SVNKLDTATV ASLGEAIGVL EQQSDLKGLL LRSNKAAFIV GADITEFLSL FLVPEEQLSQ WLHFANSVFN RLEDLPVPTI AAVNGYALGG GCECVLATDY RLATPDLRIG LPETKLGIMP GFGGSVRMPR MLGADSALEI IAAGKDVGAD QALKIGLVDG VVKAEKLVEG AKAVLRQAIN GDLDWKAKRQ PKLEPLKLSK IEATMSFTIA KGMVAQTAGK HYPAPITAVK TIEAAARFGR EEALNLENKS FVPLAHTNEA RALVGIFLND QYVKGKAKKL TKDVETPKQA AVLGAGIMGG GIAYQSAWKG VPVVMKDIND KSLTLGMTEA AKLLNKQLER GKIDGLKLAG VISTIHPTLD YAGFDRVDIV VEAVVENPKV KKAVLAETEQ KVRQDTVLAS NTSTIPISEL ANALERPENF CGMHFFNPVH RMPLVEIIRG EKSSDETIAK VVAWASKMGK TPIVVNDCPG FFVNRVLFPY FAGFSQLLRD GADFRKIDKV MEKQFGWPMG PAYLLDVVGI DTAHHAQAVM AAGFPQRMQK DYRDAIDALF DANRFGQKNG LGFWRYKEDS KGKPKKEEDA AVEDLLAEVS QPKRDFSEEE IIARMMIPMV NEVVRCLEEG IIATPAEADM ALVYGLGFPP FHGGAFRWLD TLGSAKYLDM AQQYQHLGPL YEVPEGLRNK ARHNEPYYPP VEPARPVGDL KTA |
Entity #1433 | Name: EcTFE-alpha / Type: protein / Description: Fatty acid oxidation complex subunit alpha / Formula weight: 81.206 / Num. of mol.: 1 / Source: Escherichia coli (strain K12) / References: UniProt: P21177 Sequence: MGSSHHHHHH SQDPMLYKGD TLYLDWLEDG IAELVFDAPG SVNKLDTATV ASLGEAIGVL EQQSDLKGLL LRSNKAAFIV GADITEFLSL FLVPEEQLSQ WLHFANSVFN RLEDLPVPTI AAVNGYALGG GCECVLATDY RLATPDLRIG LPETKLGIMP GFGGSVRMPR ...Sequence: MGSSHHHHHH SQDPMLYKGD TLYLDWLEDG IAELVFDAPG SVNKLDTATV ASLGEAIGVL EQQSDLKGLL LRSNKAAFIV GADITEFLSL FLVPEEQLSQ WLHFANSVFN RLEDLPVPTI AAVNGYALGG GCECVLATDY RLATPDLRIG LPETKLGIMP GFGGSVRMPR MLGADSALEI IAAGKDVGAD QALKIGLVDG VVKAEKLVEG AKAVLRQAIN GDLDWKAKRQ PKLEPLKLSK IEATMSFTIA KGMVAQTAGK HYPAPITAVK TIEAAARFGR EEALNLENKS FVPLAHTNEA RALVGIFLND QYVKGKAKKL TKDVETPKQA AVLGAGIMGG GIAYQSAWKG VPVVMKDIND KSLTLGMTEA AKLLNKQLER GKIDGLKLAG VISTIHPTLD YAGFDRVDIV VEAVVENPKV KKAVLAETEQ KVRQDTVLAS NTSTIPISEL ANALERPENF CGMHFFNPVH RMPLVEIIRG EKSSDETIAK VVAWASKMGK TPIVVNDCPG FFVNRVLFPY FAGFSQLLRD GADFRKIDKV MEKQFGWPMG PAYLLDVVGI DTAHHAQAVM AAGFPQRMQK DYRDAIDALF DANRFGQKNG LGFWRYKEDS KGKPKKEEDA AVEDLLAEVS QPKRDFSEEE IIARMMIPMV NEVVRCLEEG IIATPAEADM ALVYGLGFPP FHGGAFRWLD TLGSAKYLDM AQQYQHLGPL YEVPEGLRNK ARHNEPYYPP VEPARPVGDL KTA |
Entity #1434 | Name: EcTFE-beta / Type: protein / Description: 3-ketoacyl-CoA thiolase FadA (beta subunit) / Formula weight: 40.876 / Num. of mol.: 2 / Source: Escherichia coli (strain K12) / References: UniProt: P21151 Sequence: MEQVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPALEAAAL DDIYWGCVQQ TLEQGFNIAR NAALLAEVPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QACLVGGVEH MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLARMHGI SREMQDAFAA ...Sequence: MEQVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPALEAAAL DDIYWGCVQQ TLEQGFNIAR NAALLAEVPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QACLVGGVEH MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLARMHGI SREMQDAFAA RSHARAWAAT QSAAFKNEII PTGGHDADGV LKQFNYDEVI RPETTVEALA TLRPAFDPVN GMVTAGTSSA LSDGAAAMLV MSESRAHELG LKPRARVRSM AVVGCDPSIM GYGPVPASKL ALKKAGLSAS DIGVFEMNEA FAAQILPCIK DLGLIEQIDE KINLNGGAIA LGHPLGCSGA RISTTLLNLM ERKDVQFGLA TMCIGLGQGI ATVFERV |
-Experimental information
Beam | Instrument name: Diamond Light Source B21 / City: Didcot / 国: UK / Shape: 1 x 5 mm / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 4.014 mm | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 2M | ||||||||||||||||||||||||||||||
Scan | Title: Escherichia coli aerobic fatty acid beta-oxidation trifunctional enzyme complex Measurement date: May 30, 2017 / Storage temperature: 4 °C / Cell temperature: 20 °C / Exposure time: 3 sec. / Number of frames: 540 / Unit: 1/A /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 692 /
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Result | Type of curve: sec /
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