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==Crystal Structure of Enoyl-CoA Hydratase from Thermus Thermophilus HB8== | |||
<StructureSection load='1uiy' size='340' side='right'caption='[[1uiy]], [[Resolution|resolution]] 2.85Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1uiy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UIY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1uiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uiy OCA], [https://pdbe.org/1uiy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uiy RCSB], [https://www.ebi.ac.uk/pdbsum/1uiy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uiy ProSAT], [https://www.topsan.org/Proteins/RSGI/1uiy TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ECH_THET8 ECH_THET8] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ui/1uiy_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uiy ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fatty-acid degradation is an oxidative process that involves four enzymatic steps and is referred to as the beta-oxidation pathway. During this process, long-chain acyl-CoAs are broken down into acetyl-CoA, which enters the mitochondrial tricarboxylic acid (TCA) cycle, resulting in the production of energy in the form of ATP. Enoyl-CoA hydratase (ECH) catalyzes the second step of the beta-oxidation pathway by the syn addition of water to the double bond between C2 and C3 of a 2-trans-enoyl-CoA, resulting in the formation of a 3-hydroxyacyl CoA. Here, the crystal structure of ECH from Thermus thermophilus HB8 (TtECH) is reported at 2.85 A resolution. TtECH forms a hexamer as a dimer of trimers, and wide clefts are uniquely formed between the two trimers. Although the overall structure of TtECH is similar to that of a hexameric ECH from Rattus norvegicus (RnECH), there is a significant shift in the positions of the helices and loops around the active-site region, which includes the replacement of a longer alpha3 helix with a shorter alpha-helix and 310-helix in RnECH. Additionally, one of the catalytic residues of RnECH, Glu144 (numbering based on the RnECH enzyme), is replaced by a glycine in TtECH, while the other catalytic residue Glu164, as well as Ala98 and Gly141 that stabilize the enolate intermediate, is conserved. Their putative ligand-binding sites and active-site residue compositions are dissimilar. | |||
Crystal structure of enoyl-CoA hydratase from Thermus thermophilus HB8.,Padavattan S, Jos S, Gogoi H, Bagautdinov B Acta Crystallogr F Struct Biol Commun. 2021 May 1;77(Pt 5):148-155. doi:, 10.1107/S2053230X21004593. Epub 2021 May 4. PMID:33949975<ref>PMID:33949975</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1uiy" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Enoyl-CoA hydratase 3D structures|Enoyl-CoA hydratase 3D structures]] | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Bagautdinov | [[Category: Bagautdinov B]] | ||
[[Category: Kuramitsu | [[Category: Kuramitsu S]] | ||
[[Category: Miyano | [[Category: Miyano M]] | ||
[[Category: Tahirov TH]] | |||
[[Category: Tahirov | [[Category: Yokoyama S]] | ||
[[Category: Yokoyama | |||
Latest revision as of 03:33, 21 November 2024
Crystal Structure of Enoyl-CoA Hydratase from Thermus Thermophilus HB8Crystal Structure of Enoyl-CoA Hydratase from Thermus Thermophilus HB8
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFatty-acid degradation is an oxidative process that involves four enzymatic steps and is referred to as the beta-oxidation pathway. During this process, long-chain acyl-CoAs are broken down into acetyl-CoA, which enters the mitochondrial tricarboxylic acid (TCA) cycle, resulting in the production of energy in the form of ATP. Enoyl-CoA hydratase (ECH) catalyzes the second step of the beta-oxidation pathway by the syn addition of water to the double bond between C2 and C3 of a 2-trans-enoyl-CoA, resulting in the formation of a 3-hydroxyacyl CoA. Here, the crystal structure of ECH from Thermus thermophilus HB8 (TtECH) is reported at 2.85 A resolution. TtECH forms a hexamer as a dimer of trimers, and wide clefts are uniquely formed between the two trimers. Although the overall structure of TtECH is similar to that of a hexameric ECH from Rattus norvegicus (RnECH), there is a significant shift in the positions of the helices and loops around the active-site region, which includes the replacement of a longer alpha3 helix with a shorter alpha-helix and 310-helix in RnECH. Additionally, one of the catalytic residues of RnECH, Glu144 (numbering based on the RnECH enzyme), is replaced by a glycine in TtECH, while the other catalytic residue Glu164, as well as Ala98 and Gly141 that stabilize the enolate intermediate, is conserved. Their putative ligand-binding sites and active-site residue compositions are dissimilar. Crystal structure of enoyl-CoA hydratase from Thermus thermophilus HB8.,Padavattan S, Jos S, Gogoi H, Bagautdinov B Acta Crystallogr F Struct Biol Commun. 2021 May 1;77(Pt 5):148-155. doi:, 10.1107/S2053230X21004593. Epub 2021 May 4. PMID:33949975[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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