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== | ==Ferric horseradish peroxidase C1A in complex with formate== | ||
Carbon monoxide, formate, and acetate interact with horseradish peroxidase | <StructureSection load='1w4w' size='340' side='right'caption='[[1w4w]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1w4w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W4W 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]] 1.55Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1w4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w4w OCA], [https://pdbe.org/1w4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w4w RCSB], [https://www.ebi.ac.uk/pdbsum/1w4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w4w ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PER1A_ARMRU PER1A_ARMRU] Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w4/1w4w_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w4w ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Carbon monoxide, formate, and acetate interact with horseradish peroxidase (HRP) by binding to subsites within the active site. These ligands also bind to catalases, but their interactions are different in the two types of enzymes. Formate (notionally the "hydrated" form of carbon monoxide) is oxidized to carbon dioxide by compound I in catalase, while no such reaction is reported to occur in HRP, and the CO complex of ferrocatalase can only be obtained indirectly. Here we describe high-resolution crystal structures for HRP in its complexes with carbon monoxide and with formate, and compare these with the previously determined HRP-acetate structure [Berglund, G. I., et al. (2002) Nature 417, 463-468]. A multicrystal X-ray data collection strategy preserved the correct oxidation state of the iron during the experiments. Absorption spectra of the crystals and electron paramagnetic resonance data for the acetate and formate complexes in solution correlate electronic states with the structural results. Formate in ferric HRP and CO in ferrous HRP bind directly to the heme iron with iron-ligand distances of 2.3 and 1.8 A, respectively. CO does not bind to the ferric iron in the crystal. Acetate bound to ferric HRP stacks parallel with the heme plane with its carboxylate group 3.6 A from the heme iron, and without an intervening solvent molecule between the iron and acetate. The positions of the oxygen atoms in the bound ligands outline a potential access route for hydrogen peroxide to the iron. We propose that interactions in this channel ensure deprotonation of the proximal oxygen before binding to the heme iron. | |||
Complexes of horseradish peroxidase with formate, acetate, and carbon monoxide.,Carlsson GH, Nicholls P, Svistunenko D, Berglund GI, Hajdu J Biochemistry. 2005 Jan 18;44(2):635-42. PMID:15641789<ref>PMID:15641789</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1w4w" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Horseradish peroxidase|Horseradish peroxidase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Armoracia rusticana]] | [[Category: Armoracia rusticana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Berglund GI]] | |||
[[Category: Berglund | [[Category: Carlsson GH]] | ||
[[Category: Carlsson | [[Category: Hajdu J]] | ||
[[Category: Hajdu | [[Category: Nicholls P]] | ||
[[Category: Nicholls | [[Category: Svistunenko D]] | ||
[[Category: Svistunenko | |||