7d2r: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='7d2r' size='340' side='right'caption='[[7d2r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='7d2r' size='340' side='right'caption='[[7d2r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7d2r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. 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>
<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]] 2.005&#8491;</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&reg;/PubMed&reg;, 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]]

Latest revision as of 22:31, 29 May 2024

Crystal structure of Agrobacterium tumefaciens aconitase X mutant - S449C/C510VCrystal structure of Agrobacterium tumefaciens aconitase X mutant - S449C/C510V

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.005Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

7d2r, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA