|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==The crystal structure of MFE1 liganded with CoA== | | ==The crystal structure of MFE1 liganded with CoA== |
| - | <StructureSection load='2x58' size='340' side='right' caption='[[2x58]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='2x58' size='340' side='right'caption='[[2x58]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x58]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X58 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x58]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X58 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zcj|1zcj]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2x58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x58 OCA], [http://pdbe.org/2x58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x58 RCSB], [http://www.ebi.ac.uk/pdbsum/2x58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x58 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=2x58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x58 OCA], [https://pdbe.org/2x58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x58 RCSB], [https://www.ebi.ac.uk/pdbsum/2x58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x58 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ECHP_RAT ECHP_RAT] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 29: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Alcohol dehydrogenase|Alcohol dehydrogenase]] | + | *[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Hiltunen, J K]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Kasaragod, P]] | + | [[Category: Hiltunen JK]] |
| - | [[Category: Kiema, T R]] | + | [[Category: Kasaragod P]] |
| - | [[Category: Venkatesan, R]] | + | [[Category: Kiema TR]] |
| - | [[Category: Wierenga, R K]] | + | [[Category: Venkatesan R]] |
| - | [[Category: Beta oxidation pathway]] | + | [[Category: Wierenga RK]] |
| - | [[Category: Fatty acid metabolism]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Lipid metabolism]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxisome]]
| + | |
| Structural highlights
Function
ECHP_RAT
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the full-length rat peroxisomal multifunctional enzyme, type 1 (rpMFE1), has been determined at 2.8 A resolution. This enzyme has three catalytic activities and two active sites. The N-terminal part has the crotonase fold, which builds the active site for the Delta(3),Delta(2)-enoyl-CoA isomerase and the Delta(2)-enoyl-CoA hydratase-1 catalytic activities, and the C-terminal part has the (3S)-hydroxyacyl-CoA dehydrogenase fold and makes the (3S)-hydroxyacyl-CoA dehydrogenase active site. rpMFE1 is a multidomain protein having five domains (A-E). The crystal structure of full-length rpMFE1 shows a flexible arrangement of the A-domain with respect to the B-E-domains. Because of a hinge region near the end of the A-domain, two different positions of the A-domain were observed for the two protein molecules (A and B) of the asymmetric unit. In the most closed conformation, the mode of binding of CoA is stabilized by domains A and B (helix-10), as seen in other crotonase fold members. Domain B, although functionally belonging to the N-terminal part, is found tightly associated with the C-terminal part, i.e. fixed to the E-domain. The two active sites of rpMFE1 are approximately 40 A apart, separated by a tunnel, characterized by an excess of positively charged side chains. Comparison of the structures of rpMFE1 with the monofunctional crotonase and (3S)-hydroxyacyl-CoA dehydrogenase superfamily enzymes, as well as with the bacterial alpha(2)beta(2)-fatty acid oxidation multienzyme complex, reveals that this tunnel could be important for substrate channeling, as observed earlier on the basis of the kinetics of rpMFE1 purified from rat liver.
Crystal structure of liganded rat peroxisomal multifunctional enzyme type 1: a flexible molecule with two interconnected active sites.,Kasaragod P, Venkatesan R, Kiema TR, Hiltunen JK, Wierenga RK J Biol Chem. 2010 Jul 30;285(31):24089-98. Epub 2010 May 12. PMID:20463028[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kasaragod P, Venkatesan R, Kiema TR, Hiltunen JK, Wierenga RK. Crystal structure of liganded rat peroxisomal multifunctional enzyme type 1: a flexible molecule with two interconnected active sites. J Biol Chem. 2010 Jul 30;285(31):24089-98. Epub 2010 May 12. PMID:20463028 doi:10.1074/jbc.M110.117606
|
