6tae: Difference between revisions
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New page: '''Unreleased structure''' The entry 6tae is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Neutron structure of ferric ascorbate peroxidase== | |||
<StructureSection load='6tae' size='340' side='right'caption='[[6tae]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6tae]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TAE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6tae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tae OCA], [https://pdbe.org/6tae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tae RCSB], [https://www.ebi.ac.uk/pdbsum/6tae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tae ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q43758_SOYBN Q43758_SOYBN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In redox metalloenzymes, the process of electron transfer often involves the concerted movement of a proton. These processes are referred to as proton-coupled electron transfer, and they underpin a wide variety of biological processes, including respiration, energy conversion, photosynthesis, and metalloenzyme catalysis. The mechanisms of proton delivery are incompletely understood, in part due to an absence of information on exact proton locations and hydrogen bonding structures in a bona fide metalloenzyme proton pathway. Here, we present a 2.1-A neutron crystal structure of the complex formed between a redox metalloenzyme (ascorbate peroxidase) and its reducing substrate (ascorbate). In the neutron structure of the complex, the protonation states of the electron/proton donor (ascorbate) and all of the residues involved in the electron/proton transfer pathway are directly observed. This information sheds light on possible proton movements during heme-catalyzed oxygen activation, as well as on ascorbate oxidation. | |||
Visualizing the protons in a metalloenzyme electron proton transfer pathway.,Kwon H, Basran J, Devos JM, Suardiaz R, van der Kamp MW, Mulholland AJ, Schrader TE, Ostermann A, Blakeley MP, Moody PCE, Raven EL Proc Natl Acad Sci U S A. 2020 Mar 9. pii: 1918936117. doi:, 10.1073/pnas.1918936117. PMID:32152099<ref>PMID:32152099</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6tae" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ascorbate peroxidase 3D structures|Ascorbate peroxidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Glycine max]] | |||
[[Category: Large Structures]] | |||
[[Category: Basran J]] | |||
[[Category: Blakeley MP]] | |||
[[Category: Devos JM]] | |||
[[Category: Kwon H]] | |||
[[Category: Moody PCE]] | |||
[[Category: Ostermann A]] | |||
[[Category: Raven EL]] | |||
[[Category: Schrader TE]] | |||
Latest revision as of 18:39, 8 September 2026
Neutron structure of ferric ascorbate peroxidase
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