7cnr: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7cnr]] is a 8 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=7CNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CNR FirstGlance]. <br>
<table><tr><td colspan='2'>[[7cnr]] is a 8 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=7CNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CNR FirstGlance]. <br>
</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></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]] 3.39&#8491;</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></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=7cnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cnr OCA], [https://pdbe.org/7cnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cnr RCSB], [https://www.ebi.ac.uk/pdbsum/7cnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cnr 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=7cnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cnr OCA], [https://pdbe.org/7cnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cnr RCSB], [https://www.ebi.ac.uk/pdbsum/7cnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cnr ProSAT]</span></td></tr>
</table>
</table>

Latest revision as of 22:30, 29 May 2024

Crystal structure of Thermococcus kodakaraensis aconitase X (apo-form)Crystal structure of Thermococcus kodakaraensis aconitase X (apo-form)

Structural highlights

7cnr is a 8 chain structure with sequence from Thermococcus kodakarensis KOD1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.39Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q5JGJ6_THEKO

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Watanabe S, Murase Y, Watanabe Y, Sakurai Y, Tajima K. Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily. Commun Biol. 2021 Jun 7;4(1):687. doi: 10.1038/s42003-021-02147-5. PMID:34099860 doi:http://dx.doi.org/10.1038/s42003-021-02147-5

7cnr, resolution 3.39Å

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OCA