7cns: Difference between revisions
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==Crystal structure of Thermococcus kodakaraensis aconitase X (holo-form)== | |||
<StructureSection load='7cns' size='340' side='right'caption='[[7cns]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7cns]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CNS 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]] 1.902Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=PMV:(3R)-3-HYDROXY-3-METHYL-5-(PHOSPHONOOXY)PENTANOIC+ACID'>PMV</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=7cns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cns OCA], [https://pdbe.org/7cns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cns RCSB], [https://www.ebi.ac.uk/pdbsum/7cns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cns ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5JGJ6_THEKO Q5JGJ6_THEKO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Aconitase superfamily members catalyze the homologous isomerization of specific substrates by sequential dehydration and hydration and contain a [4Fe-4S] cluster. However, monomeric and heterodimeric types of function unknown aconitase X (AcnX) have recently been characterized as a cis-3-hydroxy-L-proline dehydratase (AcnX(Type-I)) and mevalonate 5-phosphate dehydratase (AcnX(Type-II)), respectively. We herein elucidated the crystal structures of AcnX(Type-I) from Agrobacterium tumefaciens (AtAcnX) and AcnX(Type-II) from Thermococcus kodakarensis (TkAcnX) without a ligand and in complex with substrates. AtAcnX and TkAcnX contained the [2Fe-2S] and [3Fe-4S] clusters, respectively, conforming to UV and EPR spectroscopy analyses. The binding sites of the [Fe-S] cluster and substrate were clearlydifferent from those that were completely conserved in other aconitase enzymes; however, theoverall structural frameworks and locations of active sites were partially similar to each other.These results provide novel insights into the evolutionary scenario of the aconitase superfamilybased on the recruitment hypothesis. | |||
Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily.,Watanabe S, Murase Y, Watanabe Y, Sakurai Y, Tajima K Commun Biol. 2021 Jun 7;4(1):687. doi: 10.1038/s42003-021-02147-5. PMID:34099860<ref>PMID:34099860</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7cns" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aconitase 3D structures|Aconitase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermococcus kodakarensis KOD1]] | |||
[[Category: Murase Y]] | |||
[[Category: Watanabe S]] | |||
[[Category: Watanabe Y]] | |||
Latest revision as of 19:30, 29 May 2024
Crystal structure of Thermococcus kodakaraensis aconitase X (holo-form)
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