4yso: Difference between revisions
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==Copper nitrite reductase from Geobacillus thermodenitrificans - 0.064 MGy== | |||
<StructureSection load='4yso' size='340' side='right' caption='[[4yso]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4yso]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YSO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YSO FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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">[[4ysa|4ysa]], [[4ysc|4ysc]], [[4ysd|4ysd]], [[4yse|4yse]], [[4ysp|4ysp]], [[4ysq|4ysq]], [[4ysr|4ysr]], [[4yss|4yss]], [[4yst|4yst]], [[4ysu|4ysu]]</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=4yso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yso OCA], [http://pdbe.org/4yso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yso RCSB], [http://www.ebi.ac.uk/pdbsum/4yso PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Serial femtosecond crystallography (SFX) has enabled the damage-free structural determination of metalloenzymes and filled the gaps of our knowledge between crystallographic and spectroscopic data. Crystallographers, however, scarcely know whether the rising technique provides truly new structural insights into mechanisms of metalloenzymes partly because of limited resolutions. Copper nitrite reductase (CuNiR), which converts nitrite to nitric oxide in denitrification, has been extensively studied by synchrotron radiation crystallography (SRX). Although catalytic Cu (Type 2 copper (T2Cu)) of CuNiR had been suspected to tolerate X-ray photoreduction, we here showed that T2Cu in the form free of nitrite is reduced and changes its coordination structure in SRX. Moreover, we determined the completely oxidized CuNiR structure at 1.43 A resolution with SFX. Comparison between the high-resolution SFX and SRX data revealed the subtle structural change of a catalytic His residue by X-ray photoreduction. This finding, which SRX has failed to uncover, provides new insight into the reaction mechanism of CuNiR. | |||
Redox-coupled structural changes in nitrite reductase revealed by serial femtosecond and microfocus crystallography.,Fukuda Y, Tse KM, Suzuki M, Diederichs K, Hirata K, Nakane T, Sugahara M, Nango E, Tono K, Joti Y, Kameshima T, Song C, Hatsui T, Yabashi M, Nureki O, Matsumura H, Inoue T, Iwata S, Mizohata E J Biochem. 2016 Jan 14. pii: mvv133. PMID:26769972<ref>PMID:26769972</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4yso" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Diederichs, K]] | [[Category: Diederichs, K]] | ||
[[Category: Fukuda, Y]] | [[Category: Fukuda, Y]] | ||
[[Category: Hatsui, T]] | [[Category: Hatsui, T]] | ||
[[Category: | [[Category: Hirata, K]] | ||
[[Category: | [[Category: Inoue, T]] | ||
[[Category: Iwata, S]] | [[Category: Iwata, S]] | ||
[[Category: Joti, Y]] | [[Category: Joti, Y]] | ||
[[Category: Kameshima, T]] | |||
[[Category: Matsumura, H]] | [[Category: Matsumura, H]] | ||
[[Category: | [[Category: Mizohata, E]] | ||
[[Category: Nakane, T]] | |||
[[Category: Nango, E]] | |||
[[Category: Nureki, O]] | |||
[[Category: Song, C]] | |||
[[Category: Sugahara, M]] | [[Category: Sugahara, M]] | ||
[[Category: | [[Category: Suzuki, M]] | ||
[[Category: Tono, K]] | |||
[[Category: Tse, K M]] | |||
[[Category: Yabashi, M]] | |||
[[Category: Copper]] | |||
[[Category: Nitrite]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Reductase]] | |||
Revision as of 21:10, 26 February 2016
Copper nitrite reductase from Geobacillus thermodenitrificans - 0.064 MGyCopper nitrite reductase from Geobacillus thermodenitrificans - 0.064 MGy
Structural highlights
Publication Abstract from PubMedSerial femtosecond crystallography (SFX) has enabled the damage-free structural determination of metalloenzymes and filled the gaps of our knowledge between crystallographic and spectroscopic data. Crystallographers, however, scarcely know whether the rising technique provides truly new structural insights into mechanisms of metalloenzymes partly because of limited resolutions. Copper nitrite reductase (CuNiR), which converts nitrite to nitric oxide in denitrification, has been extensively studied by synchrotron radiation crystallography (SRX). Although catalytic Cu (Type 2 copper (T2Cu)) of CuNiR had been suspected to tolerate X-ray photoreduction, we here showed that T2Cu in the form free of nitrite is reduced and changes its coordination structure in SRX. Moreover, we determined the completely oxidized CuNiR structure at 1.43 A resolution with SFX. Comparison between the high-resolution SFX and SRX data revealed the subtle structural change of a catalytic His residue by X-ray photoreduction. This finding, which SRX has failed to uncover, provides new insight into the reaction mechanism of CuNiR. Redox-coupled structural changes in nitrite reductase revealed by serial femtosecond and microfocus crystallography.,Fukuda Y, Tse KM, Suzuki M, Diederichs K, Hirata K, Nakane T, Sugahara M, Nango E, Tono K, Joti Y, Kameshima T, Song C, Hatsui T, Yabashi M, Nureki O, Matsumura H, Inoue T, Iwata S, Mizohata E J Biochem. 2016 Jan 14. pii: mvv133. PMID:26769972[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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