View source for 5ok4


==Crystal structure of native [Fe]-hydrogenase Hmd from Methanothermobacter marburgensis inactivated by O2.==
<StructureSection load='5ok4' size='340' side='right'caption='[[5ok4]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ok4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_marburgensis_str._Marburg Methanothermobacter marburgensis str. Marburg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OK4 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]] 1.29&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FEG:5-O-[(S)-{[2-(CARBOXYMETHYL)-6-HYDROXY-3,5-DIMETHYLPYRIDIN-4-YL]OXY}(HYDROXY)PHOSPHORYL]GUANOSINE'>FEG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5ok4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ok4 OCA], [https://pdbe.org/5ok4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ok4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ok4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ok4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HMD_METTM HMD_METTM] Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mono-iron hydrogenase ([Fe]-hydrogenase) reversibly catalyzes the transfer of a hydride ion from H2 to methenyltetrahydromethanopterin (methenyl-H4 MPT(+) ) to form methylene-H4 MPT. Its iron guanylylpyridinol (FeGP) cofactor plays a key role in H2 activation. Evidence is presented for O2 sensitivity of [Fe]-hydrogenase under turnover conditions in the presence of reducing substrates, methylene-H4 MPT or methenyl-H4 MPT(+) /H2 . Only then, H2 O2 is generated, which decomposes the FeGP cofactor; as demonstrated by spectroscopic analyses and the crystal structure of the deactivated enzyme. O2 reduction to H2 O2 requires a reductant, which can be a catalytic intermediate transiently formed during the [Fe]-hydrogenase reaction. The most probable candidate is an iron hydride species; its presence has already been predicted by theoretical studies of the catalytic reaction. The findings support predictions because the same type of reduction reaction is described for ruthenium hydride complexes that hydrogenate polar compounds.

Dioxygen Sensitivity of [Fe]-Hydrogenase in the Presence of Reducing Substrates.,Huang G, Wagner T, Ermler U, Bill E, Ataka K, Shima S Angew Chem Int Ed Engl. 2018 Feb 20. doi: 10.1002/anie.201712293. PMID:29462510<ref>PMID:29462510</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ok4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanothermobacter marburgensis str. Marburg]]
[[Category: Ataka K]]
[[Category: Bill E]]
[[Category: Ermler U]]
[[Category: Huang G]]
[[Category: Shima S]]
[[Category: Wagner T]]