6xv4: Difference between revisions

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 <StructureSection load='6xv4' size='340' side='right'caption='[[6xv4]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6xv4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XV4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XV4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6xv4]] 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=6XV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XV4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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]] 1.9&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">apx1, GLYMA_U021900 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine hispida])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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/L-ascorbate_peroxidase L-ascorbate peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11] </span></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=6xv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xv4 OCA], [https://pdbe.org/6xv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xv4 RCSB], [https://www.ebi.ac.uk/pdbsum/6xv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xv4 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xv4 OCA], [http://pdbe.org/6xv4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xv4 RCSB], [http://www.ebi.ac.uk/pdbsum/6xv4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xv4 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/Q43758_SOYBN Q43758_SOYBN]
-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>
+==See Also==
+*[[Ascorbate peroxidase 3D structures|Ascorbate peroxidase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6xv4" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Glycine hispida]]
+[[Category: Glycine max]]
-[[Category: L-ascorbate peroxidase]]
 [[Category: Large Structures]]
-[[Category: Basran, J]]
+[[Category: Basran J]]
-[[Category: Blakeley, M P]]
+[[Category: Blakeley MP]]
-[[Category: Devos, J M]]
+[[Category: Devos JM]]
-[[Category: Kwon, H]]
+[[Category: Kwon H]]
-[[Category: Moody, P C.E]]
+[[Category: Moody PCE]]
-[[Category: Ostermann, A]]
+[[Category: Ostermann A]]
-[[Category: Raven, E L]]
+[[Category: Raven EL]]
-[[Category: Schrader, T E]]
+[[Category: Schrader TE]]
-[[Category: Ascorbate peroxidase]]
-[[Category: Heme peroxidase]]
-[[Category: Neutron crystallography]]
-[[Category: Oxidoreductase]]
-[[Category: Proton pathway]]