7q4g: Difference between revisions

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New page: '''Unreleased structure''' The entry 7q4g is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 7q4g is ON HOLD
==Structure of coproheme decarboxylase from Corynebacterium dipththeriae Y135A mutant in complex with coproheme==
<StructureSection load='7q4g' size='340' side='right'caption='[[7q4g]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q4G 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]] 1.82&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEC:1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC+ACID+FERROUS+COMPLEX'>FEC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=7q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q4g OCA], [https://pdbe.org/7q4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q4g RCSB], [https://www.ebi.ac.uk/pdbsum/7q4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q4g ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The oxidative decarboxylation of coproheme to form heme b by coproheme decarboxylase is a stereospecific two-step reaction. In the first step, the propionate at position two (p2) is cleaved off the pyrrole ring A to form a vinyl group at this position. Subsequently, the propionate at position four (p4) on pyrrole ring B is cleaved off and heme b is formed. In this study, we attempted to engineer coproheme decarboxylase from Corynebacterium diphtheriae to alter the stereospecificity of this reaction. By introducing a tyrosine residue in proximity to the propionate at position 4, we were able to create a new radical center in the active site. However, the artificial Tyr183(*) radical could not be shown to catalyze any decarboxylation.


Authors:  
Initial Steps to Engineer Coproheme Decarboxylase to Obtain Stereospecific Monovinyl, Monopropionyl Deuterohemes.,Michlits H, Valente N, Mlynek G, Hofbauer S Front Bioeng Biotechnol. 2022 Jan 24;9:807678. doi: 10.3389/fbioe.2021.807678., eCollection 2021. PMID:35141216<ref>PMID:35141216</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7q4g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Hofbauer S]]
[[Category: Michlits H]]
[[Category: Mlynek G]]
[[Category: Valente N]]
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