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==X-ray structure of the doubly hydroxylated iron complex-NikA species, NikA1/O2== | |||
<StructureSection load='3mw0' size='340' side='right' caption='[[3mw0]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3mw0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MW0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BHR:2-[2-[CARBOXYMETHYL-[(2-HYDROXYPHENYL)METHYL]AMINO]ETHYL-[(2,3-DIHYDROXYPHENYL)METHYL]AMINO]ETHANOIC+ACID'>BHR</scene>, <scene name='pdbligand=DTD:DITHIANE+DIOL'>DTD</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mvw|3mvw]], [[3mvy|3mvy]], [[3mvx|3mvx]], [[3mvz|3mvz]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nikA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nickel-transporting_ATPase Nickel-transporting ATPase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mw0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mw0 RCSB], [http://www.ebi.ac.uk/pdbsum/3mw0 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/NIKA_ECOLI NIKA_ECOLI]] Involved in a nickel transport system, probably represents the nickel binder. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Chemical 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<ref>PMID:21107372</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Nickel-transporting ATPase]] | [[Category: Nickel-transporting ATPase]] | ||
[[Category: Bochot, C | [[Category: Bochot, C]] | ||
[[Category: Carpentier, P | [[Category: Carpentier, P]] | ||
[[Category: Cavazza, C | [[Category: Cavazza, C]] | ||
[[Category: Cherrier, M V | [[Category: Cherrier, M V]] | ||
[[Category: Fontecilla-Camps, J C | [[Category: Fontecilla-Camps, J C]] | ||
[[Category: Marchi-Delapierre, C | [[Category: Marchi-Delapierre, C]] | ||
[[Category: Martin, L | [[Category: Martin, L]] | ||
[[Category: Menage, S | [[Category: Menage, S]] | ||
[[Category: Rousselot-Pailley, P | [[Category: Rousselot-Pailley, P]] | ||
[[Category: Protein-bound iron complex]] | [[Category: Protein-bound iron complex]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 06:29, 25 December 2014
X-ray structure of the doubly hydroxylated iron complex-NikA species, NikA1/O2X-ray structure of the doubly hydroxylated iron complex-NikA species, NikA1/O2
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. References
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