5ytm: Difference between revisions
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==C135A mutant of copper-containing nitrite reductase from Geobacillus thermodenitrificans determined by in-ouse source== | |||
<StructureSection load='5ytm' size='340' side='right' caption='[[5ytm]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ytm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YTM FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] </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=5ytm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ytm OCA], [http://pdbe.org/5ytm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ytm RCSB], [http://www.ebi.ac.uk/pdbsum/5ytm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ytm ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Copper-containing nitrite reductases (CuNIRs) are multifunctional enzymes that catalyse the one-electron reduction of nitrite (NO2(-)) to nitric oxide (NO) and the two-electron reduction of dioxygen (O2) to hydrogen peroxide (H2O2). In contrast to the mechanism of nitrite reduction, that of dioxygen reduction is poorly understood. Here, results from anaerobic synchrotron-radiation crystallography (SRX) and aerobic in-house radiation crystallography (iHRX) with a CuNIR from the thermophile Geobacillus thermodenitrificans (GtNIR) support the hypothesis that the dioxygen present in an aerobically manipulated crystal can bind to the catalytic type 2 copper (T2Cu) site of GtNIR during SRX experiments. The anaerobic SRX structure showed a dual conformation of one water molecule as an axial ligand in the T2Cu site, while previous aerobic SRX GtNIR structures were refined as diatomic molecule-bound states. Moreover, an SRX structure of the C135A mutant of GtNIR with peroxide bound to the T2Cu atom was determined. The peroxide molecule was mainly observed in a side-on binding manner, with a possible minor end-on conformation. The structures provide insights into dioxygen chemistry in CuNIRs and hence help to unmask the other face of CuNIRs. | |||
Crystallographic study of dioxygen chemistry in a copper-containing nitrite reductase from Geobacillus thermodenitrificans.,Fukuda Y, Matsusaki T, Tse KM, Mizohata E, Murphy MEP, Inoue T Acta Crystallogr D Struct Biol. 2018 Aug 1;74(Pt 8):769-777. doi:, 10.1107/S2059798318010082. Epub 2018 Jul 24. PMID:30082512<ref>PMID:30082512</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ytm" style="background-color:#fffaf0;"></div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Fukuda, Y]] | |||
[[Category: Inoue, T]] | [[Category: Inoue, T]] | ||
[[Category: Matsusaki, T]] | [[Category: Matsusaki, T]] | ||
[[Category: Mizohata, E]] | |||
[[Category: Murphy, M E.P]] | |||
[[Category: Tse, K M]] | |||
[[Category: Copper]] | |||
[[Category: Nitrite reductase]] | |||
[[Category: Oxidoreductase]] | |||