6j1j: Difference between revisions
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==Crystal structure of HypX from Aquifex aeolicus, A392F-I419F variant in complex with Tetrahydrofolic acid== | |||
<StructureSection load='6j1j' size='340' side='right'caption='[[6j1j]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6j1j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J1J 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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=6j1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j1j OCA], [https://pdbe.org/6j1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j1j RCSB], [https://www.ebi.ac.uk/pdbsum/6j1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j1j ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O67224_AQUAE O67224_AQUAE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Several accessory proteins are required for the assembly of the metal centers in hydrogenases. In NiFe-hydrogenases, CO and CN(-) are coordinated to the Fe in the NiFe dinuclear cluster of the active center. Though these diatomic ligands are biosynthesized enzymatically, detail mechanisms of their biosynthesis remain unclear. Here, we report the structural characterization of HypX responsible for CO biosynthesis to assemble the active site of NiFe hydrogenase. CoA is constitutionally bound in HypX. Structural characterization of HypX suggests that the formyl-group transfer will take place from N(10)-formyl-THF to CoA to form formyl-CoA in the N-terminal domain of HypX, followed by decarbonylation of formyl-CoA to produce CO in the C-terminal domain though the direct experimental results are not available yet. The conformation of CoA accommodated in the continuous cavity connecting the N- and C-terminal domains will interconvert between the extended and the folded conformations for HypX catalysis. | |||
Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase.,Muraki N, Ishii K, Uchiyama S, Itoh SG, Okumura H, Aono S Commun Biol. 2019 Oct 18;2:385. doi: 10.1038/s42003-019-0631-z. eCollection 2019. PMID:31646188<ref>PMID:31646188</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6j1j" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aquifex aeolicus VF5]] | |||
[[Category: Large Structures]] | |||
[[Category: Aono S]] | |||
[[Category: Muraki N]] | |||
Latest revision as of 09:58, 22 November 2023
Crystal structure of HypX from Aquifex aeolicus, A392F-I419F variant in complex with Tetrahydrofolic acid
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