3cf4: Difference between revisions
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== | ==Structure of the CODH component of the M. barkeri ACDS complex== | ||
[[3cf4]] is a 2 chain structure with sequence from [ | <StructureSection load='3cf4' size='340' side='right'caption='[[3cf4]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3cf4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_barkeri Methanosarcina barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CF4 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=3cf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cf4 OCA], [https://pdbe.org/3cf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cf4 RCSB], [https://www.ebi.ac.uk/pdbsum/3cf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cf4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ACDA1_METBF ACDA1_METBF] Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.[HAMAP-Rule:MF_01137]<ref>PMID:6425262</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/cf/3cf4_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=3cf4 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ni-dependent carbon monoxide dehydrogenases (Ni-CODHs) are a diverse family of enzymes that catalyze reversible CO:CO(2) oxidoreductase activity in acetogens, methanogens, and some CO-using bacteria. Crystallography of Ni-CODHs from CO-using bacteria and acetogens has revealed the overall fold of the Ni-CODH core and has suggested structures for the C cluster that mediates CO:CO(2) interconversion. Despite these advances, the mechanism of CO oxidation has remained elusive. Herein, we report the structure of a distinct class of Ni-CODH from methanogenic archaea: the alpha(2)epsilon(2) component from the alpha(8)beta(8)gamma(8)delta(8)epsilon(8) CODH/acetyl-CoA decarbonylase/synthase complex, an enzyme responsible for the majority of biogenic methane production on Earth. The structure of this Ni-CODH component provides support for a hitherto unobserved state in which both CO and H(2)O/OH(-) bind to the Ni and the exogenous FCII iron of the C cluster, respectively, and offers insight into the structures and functional roles of the epsilon-subunit and FeS domain not present in nonmethanogenic Ni-CODHs. | |||
Structure of the alpha2epsilon2 Ni-dependent CO dehydrogenase component of the Methanosarcina barkeri acetyl-CoA decarbonylase/synthase complex.,Gong W, Hao B, Wei Z, Ferguson DJ Jr, Tallant T, Krzycki JA, Chan MK Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9558-63. Epub 2008 Jul 9. PMID:18621675<ref>PMID:18621675</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3cf4" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Acetyl-CoA synthase|Acetyl-CoA synthase]] | *[[Acetyl-CoA synthase 3D structures|Acetyl-CoA synthase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanosarcina barkeri]] | [[Category: Methanosarcina barkeri]] | ||
[[Category: Chan | [[Category: Chan MK]] | ||
[[Category: Ferguson | [[Category: Ferguson Jr DJ]] | ||
[[Category: Gong | [[Category: Gong W]] | ||
[[Category: Hao | [[Category: Hao B]] | ||
[[Category: Krzycki | [[Category: Krzycki JA]] | ||
[[Category: Tallant | [[Category: Tallant T]] | ||
[[Category: Wei | [[Category: Wei Z]] | ||
Latest revision as of 09:00, 13 August 2026
Structure of the CODH component of the M. barkeri ACDS complex
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