View source for 6hux


==HmdII from Methanocaldococcus jannaschii reconstitued with Fe-guanylylpyridinol (FeGP) cofactor and co-crystallized with methenyl-tetrahydromethanopterin at 2.5 A resolution==
<StructureSection load='6hux' size='340' side='right'caption='[[6hux]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HUX 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]] 2.5&#8491;</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=E4M:1-{4-[(6S,6aR,7R)-3-amino-6,7-dimethyl-1-oxo-1,2,5,6,6a,7-hexahydro-8H-imidazo[1,5-f]pteridin-10-ium-8-yl]phenyl}-1-deoxy-5-O-{5-O-[(S)-{[(1S)-1,3-dicarboxypropyl]oxy}(hydroxy)phosphoryl]-alpha-D-ribofuranosyl}-D-ribitol'>E4M</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE9:IRON-GUANYLYL+PYRIDINOL+COFACTOR'>FE9</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6hux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hux OCA], [https://pdbe.org/6hux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hux RCSB], [https://www.ebi.ac.uk/pdbsum/6hux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hux ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HMDY_METJA HMDY_METJA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
[Fe]-hydrogenase (Hmd) catalyzes the reversible hydrogenation of methenyl-tetrahydromethanopterin (methenyl-H4MPT+) with H2. H4MPT is a C1-carrier of methanogenic archaea. One bacterial genus, Desulfurobacterium, contains putative genes for the Hmd paralog (HmdII) and the HcgA-G proteins. The latter are involved in biosynthesis of the prosthetic group of Hmd, the iron-guanylylpyridinol (FeGP) cofactor. This finding is intriguing because Hmd and HmdII strictly use H4MPT derivatives that are absent in most bacteria. We identified the presence of the FeGP cofactor in D. thermolithotrophum. The bacterial HmdII reconstituted with the FeGP cofactor catalyzed the enzyme reactions using the tetrahydrofolate derivatives, which are the bacterial C1 carrier, albeit with low enzymatic activities. Crystal structure provided the basis for how the enzyme was adapted to the bacterial C1-carrier. This finding has impact on future biotechnology by developing the Hmd variants functioning in Bacteria.

The bacterial [Fe]-hydrogenase paralog uses tetrahydrofolate derivatives as substrates.,Watanabe T, Wagner T, Huang G, Kahnt J, Ataka K, Ermler U, Shima S Angew Chem Int Ed Engl. 2019 Jan 2. doi: 10.1002/anie.201813465. PMID:30600878<ref>PMID:30600878</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6hux" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii DSM 2661]]
[[Category: Ataka K]]
[[Category: Ermler U]]
[[Category: Huang G]]
[[Category: Kahnt J]]
[[Category: Shima S]]
[[Category: Wagner T]]
[[Category: Watanabe T]]