|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of full-length peroxisomal multifunctional enzyme type 2 from Drosophila melanogaster== | | ==Structure of full-length peroxisomal multifunctional enzyme type 2 from Drosophila melanogaster== |
| - | <StructureSection load='3oml' size='340' side='right' caption='[[3oml]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='3oml' size='340' side='right'caption='[[3oml]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3oml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OML FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3oml]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OML FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG3415, Dmel_CG3415 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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]] 2.15Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oml OCA], [http://pdbe.org/3oml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oml RCSB], [http://www.ebi.ac.uk/pdbsum/3oml PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oml 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=3oml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oml OCA], [https://pdbe.org/3oml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oml RCSB], [https://www.ebi.ac.uk/pdbsum/3oml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oml ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DHB4_DROME DHB4_DROME]] Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids.<ref>PMID:21320074</ref> | + | [https://www.uniprot.org/uniprot/DHB4_DROME DHB4_DROME] Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids.<ref>PMID:21320074</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Glumoff, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Haataja, T J.K]] | + | [[Category: Glumoff T]] |
| - | [[Category: Hiltunen, J K]] | + | [[Category: Haataja TJK]] |
| - | [[Category: Koski, M K]] | + | [[Category: Hiltunen JK]] |
| - | [[Category: Hot-dog fold]] | + | [[Category: Koski MK]] |
| - | [[Category: Hydratase 2 motif]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxisome]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
DHB4_DROME Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids.[1]
Publication Abstract from PubMed
All the peroxisomal beta-oxidation pathways characterized thus far house at least one multifunctional enzyme (MFE) catalyzing two out of four reactions of the spiral. MFE type 2 proteins from various species display great variation in domain composition and predicted substrate preference. The gene CG3415 encodes for D. melanogaster MFE-2 (DmMFE-2), complements the S. cerevisiae MFE-2 deletion strain, and the recombinant protein displays both MFE-2 enzymatic activities in vitro. The resolved crystal structure is the first one for a full-length MFE-2 revealing the assembly of domains, and the data can also be transferred to structure-function studies for other MFE-2 proteins. The structure explains the necessity of dimerization. The lack of substrate channelling is proposed based on both the structural features as well as by the fact that hydration and dehydrogenation activities of MFE-2, if produced as separate enzymes, are equally efficient in catalysis as the full-length MFE-2.
Peroxisomal multifunctional enzyme type 2 from the fruit fly: dehydrogenase and hydratase act as separate entities as revealed by structure and kinetics.,Haataja TJ, Koski MK, Hiltunen JK, Glumoff T Biochem J. 2011 Feb 14. PMID:21320074[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Haataja TJ, Koski MK, Hiltunen JK, Glumoff T. Peroxisomal multifunctional enzyme type 2 from the fruit fly: dehydrogenase and hydratase act as separate entities as revealed by structure and kinetics. Biochem J. 2011 Feb 14. PMID:21320074 doi:10.1042/BJ20101661
- ↑ Haataja TJ, Koski MK, Hiltunen JK, Glumoff T. Peroxisomal multifunctional enzyme type 2 from the fruit fly: dehydrogenase and hydratase act as separate entities as revealed by structure and kinetics. Biochem J. 2011 Feb 14. PMID:21320074 doi:10.1042/BJ20101661
|
