1rm6: Difference between revisions

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{{Seed}}
[[Image:1rm6.png|left|200px]]


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==Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica==
The line below this paragraph, containing "STRUCTURE_1rm6", creates the "Structure Box" on the page.
<StructureSection load='1rm6' size='340' side='right'caption='[[1rm6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1rm6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thauera_aromatica Thauera aromatica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RM6 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1rm6|  PDB=1rm6  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rm6 OCA], [https://pdbe.org/1rm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rm6 RCSB], [https://www.ebi.ac.uk/pdbsum/1rm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rm6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HCRA_THAAR 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.<ref>PMID:9490068</ref>
== 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/rm/1rm6_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=1rm6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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 4-hydroxybenzoyl-CoA reductase from Thauera aromatica===
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<ref>PMID:15576037</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 15576037 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_15576037}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1RM6 is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Thauera_aromatica Thauera aromatica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RM6 OCA].
 
==Reference==
<ref group="xtra">PMID:15576037</ref><references group="xtra"/>
[[Category: 4-hydroxybenzoyl-CoA reductase]]
[[Category: Thauera aromatica]]
[[Category: Thauera aromatica]]
[[Category: Boll, M.]]
[[Category: Boll M]]
[[Category: Dutton, P L.]]
[[Category: Dutton PL]]
[[Category: Ermler, U.]]
[[Category: Ermler U]]
[[Category: Page, C C.]]
[[Category: Page CC]]
[[Category: Unciuleac, M.]]
[[Category: Unciuleac M]]
[[Category: Warkentin, E.]]
[[Category: Warkentin E]]
[[Category: Dimer heterotrimer]]
[[Category: Xanthine oxidase family]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 04:40:03 2009''

Latest revision as of 07:03, 13 August 2026

Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica

1rm6, resolution 1.60Å

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