View source for 6qgr


==The F420-reducing [NiFe] hydrogenase complex from Methanosarcina barkeri at the Nia-S state==
<StructureSection load='6qgr' size='340' side='right'caption='[[6qgr]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qgr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_barkeri_MS Methanosarcina barkeri MS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QGR 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]] 1.839&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=144:TRIS-HYDROXYMETHYL-METHYL-AMMONIUM'>144</scene>, <scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NFU:FORMYL[BIS(HYDROCYANATO-1KAPPAC)]IRONNICKEL(FE-NI)'>NFU</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=6qgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qgr OCA], [https://pdbe.org/6qgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qgr RCSB], [https://www.ebi.ac.uk/pdbsum/6qgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qgr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0E3LP72_METBA A0A0E3LP72_METBA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
[NiFe] hydrogenases are complex model enzymes for the reversible cleavage of dihydrogen (H 2 ). However, structural determinants of efficient H 2 binding to their [NiFe] active site are not properly understood. Here, we present crystallographic and vibrational spectroscopic insights into the unexplored structure of the H 2 -binding [NiFe] intermediate. Using an F 420 -reducing [NiFe]-hydrogenase from Methanosarcina barkeri as a model enzyme, we show that the protein backbone provides a strained chelating scaffold that tunes the [NiFe] active site for efficient H 2 binding and conversion. The protein matrix also directs H 2 diffusion to the [NiFe] site via two gas channels and allows the distribution of electrons between functional protomers through a subunit-bridging FeS cluster. Our findings emphasize the relevance of an atypical Ni coordination, thereby providing a blueprint for the design of bio-inspired H 2 conversion catalysts.

X-ray Crystallography and Vibrational Spectroscopy Reveal Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] hydrogenases.,Ilina Y, Lorent C, Katz S, Jeoung JH, Shima S, Horch M, Zebger I, Dobbek H Angew Chem Int Ed Engl. 2019 Oct 7. doi: 10.1002/anie.201908258. PMID:31591784<ref>PMID:31591784</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qgr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanosarcina barkeri MS]]
[[Category: Dobbek H]]
[[Category: Horch M]]
[[Category: Ilina Y]]
[[Category: Jeoung JH]]
[[Category: Katz S]]
[[Category: Lorent C]]
[[Category: Shima S]]
[[Category: Zebger I]]