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| | <StructureSection load='1zcj' size='340' side='right'caption='[[1zcj]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1zcj' size='340' side='right'caption='[[1zcj]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zcj]] is a 1 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=1ZCJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZCJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zcj]] is a 1 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=1ZCJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZCJ FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxyacyl-CoA_dehydrogenase 3-hydroxyacyl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.35 1.1.1.35] </span></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]] 1.9Å</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=1zcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zcj OCA], [http://pdbe.org/1zcj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zcj RCSB], [http://www.ebi.ac.uk/pdbsum/1zcj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zcj 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=1zcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zcj OCA], [https://pdbe.org/1zcj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zcj RCSB], [https://www.ebi.ac.uk/pdbsum/1zcj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zcj 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]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-hydroxyacyl-CoA dehydrogenase]] | |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hiltunen, J K]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Kiema, T R]] | + | [[Category: Hiltunen JK]] |
| - | [[Category: Taskinen, J P]] | + | [[Category: Kiema TR]] |
| - | [[Category: Wierenga, R K]] | + | [[Category: Taskinen JP]] |
| - | [[Category: Fatty acid beta oxidation]] | + | [[Category: Wierenga RK]] |
| - | [[Category: L-bifunctional enzyme]]
| + | |
| - | [[Category: Mfe-1]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxisomal multifunctional enzyme type 1]]
| + | |
| - | [[Category: Rat]]
| + | |
| 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 1.9 A structure of the C-terminal dehydrogenase part of the rat peroxisomal monomeric multifunctional enzyme type 1 (MFE-1) has been determined. In this construct (residues 260-722 and referred to as MFE1-DH) the N-terminal hydratase part of MFE-1 has been deleted. The structure of MFE1-DH shows that it consists of an N-terminal helix, followed by a Rossmann-fold domain (domain C), followed by two tightly associated helical domains (domains D and E), which have similar topology. The structure of MFE1-DH is compared with the two known homologous structures: human mitochondrial 3-hydroxyacyl-CoA dehydrogenase (HAD; sequence identity is 33%) (which is dimeric and monofunctional) and with the dimeric multifunctional alpha-chain (alphaFOM; sequence identity is 28%) of the bacterial fatty acid beta-oxidation alpha2beta2-multienzyme complex. Like MFE-1, alphaFOM has an N-terminal hydratase part and a C-terminal dehydrogenase part, and the structure comparisons show that the N-terminal helix of MFE1-DH corresponds to the alphaFOM linker helix, located between its hydratase and dehydrogenase part. It is also shown that this helix corresponds to the C-terminal helix-10 of the hydratase/isomerase superfamily, suggesting that functionally it belongs to the N-terminal hydratase part of MFE-1.
Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1.,Taskinen JP, Kiema TR, Hiltunen JK, Wierenga RK J Mol Biol. 2006 Jan 27;355(4):734-46. Epub 2005 Nov 18. PMID:16330050[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Taskinen JP, Kiema TR, Hiltunen JK, Wierenga RK. Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1. J Mol Biol. 2006 Jan 27;355(4):734-46. Epub 2005 Nov 18. PMID:16330050 doi:http://dx.doi.org/10.1016/j.jmb.2005.10.085
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