1rm6
From Proteopedia
(New page: 200px<br /><applet load="1rm6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rm6, resolution 1.60Å" /> '''Structure of 4-hydro...) |
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| - | [[Image:1rm6.gif|left|200px]]<br /><applet load="1rm6" size=" | + | [[Image:1rm6.gif|left|200px]]<br /><applet load="1rm6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rm6, resolution 1.60Å" /> | caption="1rm6, resolution 1.60Å" /> | ||
'''Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica'''<br /> | '''Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Mo-flavo-Fe/S-dependent heterohexameric protein complex | + | The Mo-flavo-Fe/S-dependent heterohexameric protein complex 4-hydroxybenzoyl-CoA reductase (4-HBCR, dehydroxylating) is a central enzyme of the anaerobic degradation of phenolic compounds and belongs to the xanthine oxidase (XO) family of molybdenum enzymes. Its X-ray structure was established at 1.6 A resolution. The most pronounced difference between 4-HBCR and other structurally characterized members of the XO family is the insertion of 40 amino acids within the beta subunit, which carries an additional [4Fe-4S] cluster at a distance of 16.5 A to the isoalloxazine ring of FAD. The architecture of 4-HBCR and concomitantly performed electron transfer rate calculations suggest an inverted electron transfer chain from the donor ferredoxin via the [4Fe-4S] cluster to the Mo over a distance of 55 A. The binding site of 4-hydroxybenzoyl-CoA is located in an 18 A long channel lined up by several aromatic side chains around the aromatic moiety, which are proposed to shield and stabilize the postulated radical intermediates during catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1RM6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thauera_aromatica Thauera aromatica] with CL, K, NA, SO4, PCD, FAD, SF4, FES and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA_reductase 4-hydroxybenzoyl-CoA reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.20 1.3.99.20] Full crystallographic information is available from [http:// | + | 1RM6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thauera_aromatica Thauera aromatica] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=PCD:'>PCD</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA_reductase 4-hydroxybenzoyl-CoA reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.20 1.3.99.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RM6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thauera aromatica]] | [[Category: Thauera aromatica]] | ||
[[Category: Boll, M.]] | [[Category: Boll, M.]] | ||
| - | [[Category: Dutton, P | + | [[Category: Dutton, P L.]] |
[[Category: Ermler, U.]] | [[Category: Ermler, U.]] | ||
| - | [[Category: Page, C | + | [[Category: Page, C C.]] |
[[Category: Unciuleac, M.]] | [[Category: Unciuleac, M.]] | ||
[[Category: Warkentin, E.]] | [[Category: Warkentin, E.]] | ||
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[[Category: xanthine oxidase family]] | [[Category: xanthine oxidase family]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:21 2008'' |
Revision as of 12:52, 21 February 2008
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Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica
Overview
The Mo-flavo-Fe/S-dependent heterohexameric protein complex 4-hydroxybenzoyl-CoA reductase (4-HBCR, dehydroxylating) is a central enzyme of the anaerobic degradation of phenolic compounds and belongs to the xanthine oxidase (XO) family of molybdenum enzymes. Its X-ray structure was established at 1.6 A resolution. The most pronounced difference between 4-HBCR and other structurally characterized members of the XO family is the insertion of 40 amino acids within the beta subunit, which carries an additional [4Fe-4S] cluster at a distance of 16.5 A to the isoalloxazine ring of FAD. The architecture of 4-HBCR and concomitantly performed electron transfer rate calculations suggest an inverted electron transfer chain from the donor ferredoxin via the [4Fe-4S] cluster to the Mo over a distance of 55 A. The binding site of 4-hydroxybenzoyl-CoA is located in an 18 A long channel lined up by several aromatic side chains around the aromatic moiety, which are proposed to shield and stabilize the postulated radical intermediates during catalysis.
About this Structure
1RM6 is a Protein complex structure of sequences from Thauera aromatica with , , , , , , , and as ligands. Active as 4-hydroxybenzoyl-CoA reductase, with EC number 1.3.99.20 Full crystallographic information is available from OCA.
Reference
Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow., Unciuleac M, Warkentin E, Page CC, Boll M, Ermler U, Structure. 2004 Dec;12(12):2249-56. PMID:15576037
Page seeded by OCA on Thu Feb 21 14:52:21 2008
Categories: 4-hydroxybenzoyl-CoA reductase | Protein complex | Thauera aromatica | Boll, M. | Dutton, P L. | Ermler, U. | Page, C C. | Unciuleac, M. | Warkentin, E. | CL | EPE | FAD | FES | K | NA | PCD | SF4 | SO4 | (a | B | C)2 | Dimer heterotrimers | Xanthine oxidase family
