4c1n
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c1n]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C1N FirstGlance]. <br> | <table><tr><td colspan='2'>[[4c1n]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C1N FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.53Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=4c1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c1n OCA], [https://pdbe.org/4c1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c1n RCSB], [https://www.ebi.ac.uk/pdbsum/4c1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c1n ProSAT]</span></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=4c1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c1n OCA], [https://pdbe.org/4c1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c1n RCSB], [https://www.ebi.ac.uk/pdbsum/4c1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c1n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/Q3ACS3_CARHZ Q3ACS3_CARHZ] | |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Thermodynamically unfavourable electron transfers are enabled by coupling to an energy-supplying reaction. How the energy is transduced from the exergonic to the endergonic process is largely unknown. Here we provide the structural basis for an energy transduction process in the reductive activation of B12-dependent methyltransferases. The transfer of one electron from an activating enzyme to the cobalamin cofactor is energetically uphill and relies on coupling to an ATPase reaction. Our results demonstrate that the key to coupling is, besides the oxidation state-dependent complex formation, the conformational gating of the electron transfer. Complex formation induces a substitution of the ligand at the electron-accepting Co ion. Addition of ATP initiates electron transfer by provoking conformational changes that destabilize the complex. We show how remodelling of the electron-accepting Co(2+) promotes ATP-dependent electron transfer; an efficient strategy not seen in other electron-transferring ATPases. | ||
| + | |||
| + | ATP-induced electron transfer by redox-selective partner recognition.,Hennig SE, Goetzl S, Jeoung JH, Bommer M, Lendzian F, Hildebrandt P, Dobbek H Nat Commun. 2014 Aug 11;5:4626. doi: 10.1038/ncomms5626. PMID:25109607<ref>PMID:25109607</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4c1n" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Acetyl-CoA synthase 3D structures|Acetyl-CoA synthase 3D structures]] | *[[Acetyl-CoA synthase 3D structures|Acetyl-CoA synthase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Corrinoid protein reactivation complex with activator
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