1rm6

From Proteopedia

(Difference between revisions)

Revision as of 06:40, 8 March 2018

Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica

Structural highlights

1rm6 is a 6 chain structure with sequence from Thauera aromatica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , , ,
Activity:	4-hydroxybenzoyl-CoA reductase, with EC number 1.3.7.9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HCRA_THAAR] Component of a complex that catalyzes the reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA. Reaction is not reversible. Is a key enzyme in the anaerobic degradation of phenolic compounds.^[1] [HCRC_THAAR] Component of a complex that catalyzes the reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA. Reaction is not reversible. Is a key enzyme in the anaerobic degradation of phenolic compounds.^[2] [HCRB_THAAR] Component of a complex that catalyzes the reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA. Reaction is not reversible. Is a key enzyme in the anaerobic degradation of phenolic compounds.^[3]

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 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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Breese K, Fuchs G. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica--prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins. Eur J Biochem. 1998 Feb 1;251(3):916-23. PMID:9490068
↑ Breese K, Fuchs G. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica--prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins. Eur J Biochem. 1998 Feb 1;251(3):916-23. PMID:9490068
↑ Breese K, Fuchs G. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica--prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins. Eur J Biochem. 1998 Feb 1;251(3):916-23. PMID:9490068
↑ Unciuleac M, Warkentin E, Page CC, Boll M, Ermler U. Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow. Structure. 2004 Dec;12(12):2249-56. PMID:15576037 doi:http://dx.doi.org/10.1016/j.str.2004.10.008

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rm6"

@@ Line 1: / Line 1: @@
 ==Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica==
 <StructureSection load='1rm6' size='340' side='right' caption='[[1rm6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PCD:(MOLYBDOPTERIN-CYTOSINE+DINUCLEOTIDE-S,S)-DIOXO-AQUA-MOLYBDENUM(V)'>PCD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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=1.3.7.9 1.3.7.9] </span></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=1rm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rm6 OCA], [http://pdbe.org/1rm6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rm6 RCSB], [http://www.ebi.ac.uk/pdbsum/1rm6 PDBsum]</span></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=1rm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rm6 OCA], [http://pdbe.org/1rm6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rm6 RCSB], [http://www.ebi.ac.uk/pdbsum/1rm6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rm6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rm/1rm6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rm/1rm6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1rm6 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1rm6

From Proteopedia

Revision as of 06:40, 8 March 2018

Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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