8qmn
From Proteopedia
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<table><tr><td colspan='2'>[[8qmn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QMN FirstGlance]. <br> | <table><tr><td colspan='2'>[[8qmn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QMN 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]] 1.48Å</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]] 1.48Å</td></tr> | ||
| - | <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=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH | + | <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=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=8qmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qmn OCA], [https://pdbe.org/8qmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qmn RCSB], [https://www.ebi.ac.uk/pdbsum/8qmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qmn 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=8qmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qmn OCA], [https://pdbe.org/8qmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qmn RCSB], [https://www.ebi.ac.uk/pdbsum/8qmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qmn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HYDE_THEMA HYDE_THEMA] Required for the maturation of the [FeFe]-hydrogenase HydA (By similarity). Catalyzes the reductive cleavage of S-adenosyl-L-methionine (in vitro), suggesting it may contribute to the biosynthesis of an essential sulfur-containing ligand that binds to the hydrogenase active site [2Fe-2S] cluster (PubMed:16137685).[UniProtKB:Q97IK9]<ref>PMID:16137685</ref> | [https://www.uniprot.org/uniprot/HYDE_THEMA HYDE_THEMA] Required for the maturation of the [FeFe]-hydrogenase HydA (By similarity). Catalyzes the reductive cleavage of S-adenosyl-L-methionine (in vitro), suggesting it may contribute to the biosynthesis of an essential sulfur-containing ligand that binds to the hydrogenase active site [2Fe-2S] cluster (PubMed:16137685).[UniProtKB:Q97IK9]<ref>PMID:16137685</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | FeFe]-hydrogenases efficiently catalyze the reversible oxidation of molecular hydrogen. Their prowess stems from the intricate H-cluster, combining a [Fe4S4] center with a binuclear iron center ([2Fe]H). In the latter, each iron atom is coordinated by a CO and CN ligand, connected by a CO and an azadithiolate ligand. The synthesis of this active site involves a unique multiprotein assembly, featuring radical SAM proteins HydG and HydE. HydG initiates the transformation of L-tyrosine into cyanide and carbon monoxide to generate complex-B, which is subsequently transferred to HydE to continue the biosynthesis of the [2Fe]H-subcluster. Due to its instability, complex-B isolation for structural or spectroscopic characterization has been elusive this far. Nevertheless, the use of a biomimetic compound of complex-B allowed circumventing the need for the HydG protein during in vitro functional investigations, implying a similar structure for complex-B. Here, we used the HydE protein as a nanocage to encapsulate and stabilize the complex-B product generated by HydG. Using X-ray crystallography, we successfully determined its structure at 1.3 A resolution. Furthermore, we demonstrated that complex-B is directly transferred from HydG to HydE, thus not being released into the solution post-synthesis, highlighting a transient interaction between the two proteins. | ||
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| - | Maturation of the [FeFe]-Hydrogenase: Direct Transfer of the (kappa3-cysteinate)FeII(CN)(CO)2 Complex-B from HydG to HydE.,Omeiri J, Martin L, Usclat A, Cherrier MV, Nicolet Y Angew Chem Int Ed Engl. 2023 Nov 14:e202314819. doi: 10.1002/anie.202314819. PMID:37962296<ref>PMID:37962296</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 8qmn" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
[FeFe]-hydrogenase maturase HydE from T. maritima - dialysis experiment - empty structure
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