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1u8v
From Proteopedia
(New page: 200px<br /><applet load="1u8v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u8v, resolution 1.6Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1u8v.jpg|left|200px]]<br /><applet load="1u8v" size=" | + | [[Image:1u8v.jpg|left|200px]]<br /><applet load="1u8v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1u8v, resolution 1.6Å" /> | caption="1u8v, resolution 1.6Å" /> | ||
'''Crystal Structure of 4-Hydroxybutyryl-CoA Dehydratase from Clostridium aminobutyricum: Radical catalysis involving a [4Fe-4S] cluster and flavin'''<br /> | '''Crystal Structure of 4-Hydroxybutyryl-CoA Dehydratase from Clostridium aminobutyricum: Radical catalysis involving a [4Fe-4S] cluster and flavin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Dehydratases catalyze the breakage of a carbon-oxygen bond leading to | + | Dehydratases catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the elimination of water. The 1.6-A resolution crystal structure of 4-hydroxybutyryl-CoA dehydratase from the gamma-aminobutyrate-fermenting Clostridium aminobutyricum represents a new class of dehydratases with an unprecedented active site architecture. A [4Fe-4S](2+) cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide (FAD) moiety. The structure provides insight into the function of these ubiquitous prosthetic groups in the chemically nonfacile, radical-mediated dehydration of 4-hydroxybutyryl-CoA. The substrate can be bound between the [4Fe-4S](2+) cluster and the FAD with both cofactors contributing to its radical activation and catalytic conversion. Our results raise interesting questions regarding the mechanism of acyl-CoA dehydrogenases, which are involved in fatty acid oxidation, and address the divergent evolution of the ancestral common gene. |
==About this Structure== | ==About this Structure== | ||
| - | 1U8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_aminobutyricum Clostridium aminobutyricum] with SF4 and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1U8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_aminobutyricum Clostridium aminobutyricum] with <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U8V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cinkaya, I.]] | [[Category: Cinkaya, I.]] | ||
[[Category: Dobbek, H.]] | [[Category: Dobbek, H.]] | ||
| - | [[Category: Martins, B | + | [[Category: Martins, B M.]] |
[[Category: Messerschmidt, A.]] | [[Category: Messerschmidt, A.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: beta-strands]] | [[Category: beta-strands]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:52 2008'' |
Revision as of 13:21, 21 February 2008
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Crystal Structure of 4-Hydroxybutyryl-CoA Dehydratase from Clostridium aminobutyricum: Radical catalysis involving a [4Fe-4S] cluster and flavin
Overview
Dehydratases catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the elimination of water. The 1.6-A resolution crystal structure of 4-hydroxybutyryl-CoA dehydratase from the gamma-aminobutyrate-fermenting Clostridium aminobutyricum represents a new class of dehydratases with an unprecedented active site architecture. A [4Fe-4S](2+) cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide (FAD) moiety. The structure provides insight into the function of these ubiquitous prosthetic groups in the chemically nonfacile, radical-mediated dehydration of 4-hydroxybutyryl-CoA. The substrate can be bound between the [4Fe-4S](2+) cluster and the FAD with both cofactors contributing to its radical activation and catalytic conversion. Our results raise interesting questions regarding the mechanism of acyl-CoA dehydrogenases, which are involved in fatty acid oxidation, and address the divergent evolution of the ancestral common gene.
About this Structure
1U8V is a Single protein structure of sequence from Clostridium aminobutyricum with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of 4-hydroxybutyryl-CoA dehydratase: radical catalysis involving a [4Fe-4S] cluster and flavin., Martins BM, Dobbek H, Cinkaya I, Buckel W, Messerschmidt A, Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15645-9. Epub 2004 Oct 20. PMID:15496473
Page seeded by OCA on Thu Feb 21 15:21:52 2008
