|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6yu9' size='340' side='right'caption='[[6yu9]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='6yu9' size='340' side='right'caption='[[6yu9]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6yu9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_autoethanogenum_dsm_10061 Clostridium autoethanogenum dsm 10061]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YU9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YU9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6yu9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_autoethanogenum_DSM_10061 Clostridium autoethanogenum DSM 10061]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YU9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=XCC:FE(4)-NI(1)-S(4)+CLUSTER'>XCC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.904Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yu9 OCA], [http://pdbe.org/6yu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yu9 RCSB], [http://www.ebi.ac.uk/pdbsum/6yu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yu9 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=XCC:FE(4)-NI(1)-S(4)+CLUSTER'>XCC</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=6yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yu9 OCA], [https://pdbe.org/6yu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yu9 RCSB], [https://www.ebi.ac.uk/pdbsum/6yu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yu9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/U5RTE2_9CLOT U5RTE2_9CLOT] [https://www.uniprot.org/uniprot/U5RSY1_9CLOT U5RSY1_9CLOT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 16: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6yu9" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6yu9" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Carbon monoxide dehydrogenase 3D structures|Carbon monoxide dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Clostridium autoethanogenum dsm 10061]] | + | [[Category: Clostridium autoethanogenum DSM 10061]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lemaire, O N]] | + | [[Category: Lemaire ON]] |
| - | [[Category: Wagner, T]] | + | [[Category: Wagner T]] |
| - | [[Category: Acetogenesis]]
| + | |
| - | [[Category: Acetogenic bacteria]]
| + | |
| - | [[Category: C1-metabolism]]
| + | |
| - | [[Category: Carbon monoxide]]
| + | |
| - | [[Category: Co-dehydrogenase/acetyl-coa synthase]]
| + | |
| - | [[Category: Gas channeling]]
| + | |
| - | [[Category: Metallo-containing protein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Waste-gas conversion]]
| + | |
| - | [[Category: X-ray crystal structure]]
| + | |
| Structural highlights
6yu9 is a 4 chain structure with sequence from Clostridium autoethanogenum DSM 10061. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.904Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
U5RTE2_9CLOT U5RSY1_9CLOT
Publication Abstract from PubMed
Clostridium autoethanogenum, the bacterial model for biological conversion of waste gases into biofuels, grows under extreme carbon-monoxide (CO) concentrations. The strictly anaerobic bacterium derives its entire cellular energy and carbon from this poisonous gas, therefore requiring efficient molecular machineries for CO-conversion. Here, we structurally and biochemically characterized the key enzyme of the CO-converting metabolism: the CO-dehydrogenase/Acetyl-CoA synthase (CODH/ACS). We obtained crystal structures of natively isolated complexes from fructose-grown and CO-grown C. autoethanogenum cultures. Both contain the same isoforms and if the overall structure adopts the classic alpha2beta2 architecture, comparable to the model enzyme from Moorella thermoacetica, the ACS binds a different position on the CODH core. The structural characterization of a proteolyzed complex and the conservation of the binding interface in close homologs rejected the possibility of a crystallization artefact. Therefore, the internal CO-channeling system, critical to transfer CO generated at the C-cluster to the ACS active site, drastically differs in the complex from C. autoethanogenum. The 1.9-A structure of the CODH alone provides an accurate picture of the new CO-routes, leading to the ACS core and reaching the surface. Increased gas accessibility would allow the simultaneous CO-oxidation and acetyl-CoA production. Biochemical experiments showed higher flexibility of the ACS subunit from C. autoethanogenum compared to M. thermoacetica, albeit monitoring similar CO-oxidation and formation rates. These results show a reshuffling of internal CO-tunnels during evolution of these Firmicutes, putatively leading to a bidirectional complex that ensure a high flux of CO-conversion toward energy conservation, acting as the main cellular powerplant.
Gas channel rerouting in a primordial enzyme: Structural insights of the carbon-monoxide dehydrogenase/acetyl-CoA synthase complex from the acetogen Clostridium autoethanogenum.,Lemaire ON, Wagner T Biochim Biophys Acta Bioenerg. 2020 Oct 17;1862(1):148330. doi:, 10.1016/j.bbabio.2020.148330. PMID:33080205[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lemaire ON, Wagner T. Gas channel rerouting in a primordial enzyme: Structural insights of the carbon-monoxide dehydrogenase/acetyl-CoA synthase complex from the acetogen Clostridium autoethanogenum. Biochim Biophys Acta Bioenerg. 2020 Oct 17;1862(1):148330. doi:, 10.1016/j.bbabio.2020.148330. PMID:33080205 doi:http://dx.doi.org/10.1016/j.bbabio.2020.148330
|
