View source for 3zch


==Ascorbate peroxidase W41A-H42M mutant==
<StructureSection load='3zch' size='340' side='right'caption='[[3zch]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zch]] 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=3ZCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZCH 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zch OCA], [https://pdbe.org/3zch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zch RCSB], [https://www.ebi.ac.uk/pdbsum/3zch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zch ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q43758_SOYBN Q43758_SOYBN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have previously demonstrated (Badyal et al., J. Biol. Chem., 2006, 281, 24512) that removal of the active site tryptophan (Trp41) in ascorbate peroxidase increases the conformational mobility of the distal histidine residue (His42) and that His42 coordinates to the iron in the oxidised W41A enzyme to give a 6-coordinate, low-spin peroxidase. In this work, we probe the conformational flexibility of the active site in more detail. We examine whether other residues (Cys, Tyr, Met) can also ligate to the heme at position 42; we find that introduction of other ligating amino acids created a cavity in the heme pocket, but that formation of 6-coordinate heme is not observed. In addition, we examine the role of Asn-71, which hydrogen bonds to His42 and tethers the distal histidine in the active site pocket; we find that removal of this hydrogen bond increases the proportion of low-spin heme. We suggest that, in addition to its well-known role in facilitating the reaction with peroxide, His42 also plays a role in defining the shape and folding of the active site pocket.

Probing the conformational mobility of the active site of a heme peroxidase.,Guimero A, Badyal SK, Leeks T, Moody PC, Raven EL Dalton Trans. 2012 Dec 3. PMID:23202589<ref>PMID:23202589</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zch" 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: Gumiero A]]
[[Category: Moody PCE]]
[[Category: Raven EL]]