View source for 6tfo


==Crystal structure of as isolated three-domain copper-containing nitrite reductase from Hyphomicrobium denitrificans strain 1NES1==
<StructureSection load='6tfo' size='340' side='right'caption='[[6tfo]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6tfo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyphomicrobium_denitrificans_1NES1 Hyphomicrobium denitrificans 1NES1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TFO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=6tfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tfo OCA], [https://pdbe.org/6tfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tfo RCSB], [https://www.ebi.ac.uk/pdbsum/6tfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tfo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/N0B9M5_9HYPH N0B9M5_9HYPH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Copper-containing nitrite reductases (CuNiRs) are found in all three kingdoms of life and play a major role in the denitrification branch of the global nitro-gen cycle where nitrate is used in place of di-oxy-gen as an electron acceptor in respiratory energy metabolism. Several C- and N-terminal redox domain tethered CuNiRs have been identified and structurally characterized during the last decade. Our understanding of the role of tethered domains in these new classes of three-domain CuNiRs, where an extra cytochrome or cupredoxin domain is tethered to the catalytic two-domain CuNiRs, has remained limited. This is further compounded by a complete lack of substrate-bound structures for these tethered CuNiRs. There is still no substrate-bound structure for any of the as-isolated wild-type tethered enzymes. Here, structures of nitrite and product-bound states from a nitrite-soaked crystal of the N-terminal cupredoxin-tethered enzyme from the Hyphomicrobium denitrificans strain 1NES1 (Hd 1NES1NiR) are provided. These, together with the as-isolated structure of the same species, provide clear evidence for the role of the N-terminal peptide bearing the conserved His27 in water-mediated anchoring of the substrate at the catalytic T2Cu site. Our data indicate a more complex role of tethering than the intuitive advantage for a partner-protein electron-transfer complex by narrowing the conformational search in such a combined system.

Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes.,Sasaki D, Watanabe TF, Eady RR, Garratt RC, Antonyuk SV, Hasnain SS IUCrJ. 2020 Apr 25;7(Pt 3):557-565. doi: 10.1107/S2052252520005230. eCollection, 2020 May 1. PMID:32431838<ref>PMID:32431838</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6tfo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hyphomicrobium denitrificans 1NES1]]
[[Category: Large Structures]]
[[Category: Antonyuk SV]]
[[Category: Eady RR]]
[[Category: Garratt RC]]
[[Category: Hasnain SS]]
[[Category: Sasaki D]]
[[Category: Watanabe TF]]