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==X-ray structure of NikA in complex with HBED== | ==X-ray structure of NikA in complex with HBED== | ||
<StructureSection load='3mz9' size='340' side='right' caption='[[3mz9]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3mz9' size='340' side='right'caption='[[3mz9]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3mz9]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3mz9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MZ9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BHN:2-[2-[CARBOXYMETHYL-[(2-HYDROXYPHENYL)METHYL]AMINO]ETHYL-[(2-HYDROXYPHENYL)METHYL]AMINO]ETHANOIC+ACID'>BHN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DTD:DITHIANE+DIOL'>DTD</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BHN:2-[2-[CARBOXYMETHYL-[(2-HYDROXYPHENYL)METHYL]AMINO]ETHYL-[(2-HYDROXYPHENYL)METHYL]AMINO]ETHANOIC+ACID'>BHN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DTD:DITHIANE+DIOL'>DTD</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mvx|3mvx]], [[3mvy|3mvy]], [[3mvz|3mvz]], [[3mw0|3mw0]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3mvx|3mvx]], [[3mvy|3mvy]], [[3mvz|3mvz]], [[3mw0|3mw0]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nikA ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nikA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nickel-transporting_ATPase Nickel-transporting ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.24 3.6.3.24] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mz9 OCA], [https://pdbe.org/3mz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mz9 RCSB], [https://www.ebi.ac.uk/pdbsum/3mz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mz9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/NIKA_ECOLI NIKA_ECOLI]] Involved in a nickel transport system, probably represents the nickel binder. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 21: | ||
</div> | </div> | ||
<div class="pdbe-citations 3mz9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3mz9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[ABC transporter 3D structures|ABC transporter 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 26: | Line 29: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
[[Category: Large Structures]] | |||
[[Category: Nickel-transporting ATPase]] | [[Category: Nickel-transporting ATPase]] | ||
[[Category: Bochot, C]] | [[Category: Bochot, C]] | ||
Revision as of 09:53, 12 May 2022
X-ray structure of NikA in complex with HBEDX-ray structure of NikA in complex with HBED
Structural highlights
Function[NIKA_ECOLI] Involved in a nickel transport system, probably represents the nickel binder. Publication Abstract from PubMedChemical reactions inside single crystals are quite rare because crystallinity is difficult to retain owing to atomic rearrangements. Protein crystals in general have a high solvent content. This allows for some molecular flexibility, which makes it possible to trap reaction intermediates of enzymatic reactions without disrupting the crystal lattice. A similar approach has not yet been fully implemented in the field of inorganic chemistry. Here, we have combined model chemistry and protein X-ray crystallography to study the intramolecular aromatic dihydroxylation by an arene-containing protein-bound iron complex. The bound complex was able to activate dioxygen in the presence of a reductant, leading to the formation of catechol as the sole product. The structure determination of four of the catalytic cycle intermediates and the end product showed that the hydroxylation reaction implicates an iron peroxo, generated by reductive O(2) activation, an intermediate already observed in iron monooxygenases. This strategy also provided unexpected mechanistic details such as the rearrangement of the iron coordination sphere on metal reduction. Crystallographic snapshots of the reaction of aromatic C-H with O(2) catalysed by a protein-bound iron complex.,Cavazza C, Bochot C, Rousselot-Pailley P, Carpentier P, Cherrier MV, Martin L, Marchi-Delapierre C, Fontecilla-Camps JC, Menage S Nat Chem. 2010 Dec;2(12):1069-76. Epub 2010 Oct 10. PMID:21107372[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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