3wnu: Difference between revisions
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New page: '''Unreleased structure''' The entry 3wnu is ON HOLD Authors: Toshiji Tada, Kei Wada, Saori Kamachi Description: The crystal structure of catalase-peroxidase, KatG, from Synechococcus ... |
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The | ==The crystal structure of catalase-peroxidase, KatG, from Synechococcus PCC7942== | ||
<StructureSection load='3wnu' size='340' side='right'caption='[[3wnu]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wnu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WNU 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]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=3wnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wnu OCA], [https://pdbe.org/3wnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wnu RCSB], [https://www.ebi.ac.uk/pdbsum/3wnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wnu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KATG_SYNE7 KATG_SYNE7] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.[HAMAP-Rule:MF_01961] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of catalase-peroxidase from Synechococcus elongatus PCC7942 (SeKatG) was solved by molecular replacement and refined to an Rwork of 16.8% and an Rfree of 20.6% at 2.2 A resolution. The asymmetric unit consisted of only one subunit of the catalase-peroxidase molecule, including a protoporphyrin IX haem moiety and two sodium ions. A typical KatG covalent adduct was formed, Met248-Tyr222-Trp94, which is a key structural element for catalase activity. The crystallographic equivalent subunit was created by a twofold symmetry operation to form the functional dimer. The overall structure of the dimer was quite similar to other KatGs. One sodium ion was located close to the proximal Trp314. The location and configuration of the proximal cation site were very similar to those of typical peroxidases such as ascorbate peroxidase. These features may provide a structural basis for the behaviour of the radical localization/delocalization during the course of the enzymatic reaction. | |||
The 2.2 A resolution structure of the catalase-peroxidase KatG from Synechococcus elongatus PCC7942.,Kamachi S, Wada K, Tamoi M, Shigeoka S, Tada T Acta Crystallogr F Struct Biol Commun. 2014 Mar;70(Pt 3):288-93. doi:, 10.1107/S2053230X14002052. Epub 2014 Feb 19. PMID:24598912<ref>PMID:24598912</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3wnu" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Catalase 3D structures|Catalase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]] | |||
[[Category: Kamachi S]] | |||
[[Category: Tada T]] | |||
[[Category: Wada K]] | |||
Latest revision as of 10:43, 13 August 2026
The crystal structure of catalase-peroxidase, KatG, from Synechococcus PCC7942
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