7d2r
From Proteopedia
(Difference between revisions)
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<StructureSection load='7d2r' size='340' side='right'caption='[[7d2r]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='7d2r' size='340' side='right'caption='[[7d2r]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D2R FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.005Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7d2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d2r OCA], [https://pdbe.org/7d2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d2r RCSB], [https://www.ebi.ac.uk/pdbsum/7d2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d2r ProSAT]</span></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=7d2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d2r OCA], [https://pdbe.org/7d2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d2r RCSB], [https://www.ebi.ac.uk/pdbsum/7d2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d2r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | == Function == | ||
- | [https://www.uniprot.org/uniprot/A0A083ZM39_RHIRD A0A083ZM39_RHIRD] | ||
- | <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> | ||
- | </div> | ||
- | <div class="pdbe-citations 7d2r" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Aconitase 3D structures|Aconitase 3D structures]] | *[[Aconitase 3D structures|Aconitase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Agrobacterium tumefaciens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Murase Y]] | [[Category: Murase Y]] | ||
[[Category: Watanabe S]] | [[Category: Watanabe S]] | ||
[[Category: Watanabe Y]] | [[Category: Watanabe Y]] |
Current revision
Crystal structure of Agrobacterium tumefaciens aconitase X mutant - S449C/C510V
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