6m8f: Difference between revisions

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-'''Unreleased structure'''
-The entry 6m8f is ON HOLD  until Paper Publication
+==Engineered sperm whale myoglobin-based carbene transferase==
+<StructureSection load='6m8f' size='340' side='right'caption='[[6m8f]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6m8f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phymc Phymc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M8F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6M8F FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 PHYMC])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6m8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m8f OCA], [http://pdbe.org/6m8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m8f RCSB], [http://www.ebi.ac.uk/pdbsum/6m8f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m8f ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MYG_PHYCD MYG_PHYCD]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Recent advances in metalloprotein engineering have led to the development of a myoglobin-based catalyst, Mb(H64V,V68A), capable of promoting the cyclopropanation of vinylarenes with high efficiency and high diastereo- and enantioselectivity. Whereas many enzymes evolved in nature often exhibit catalytic proficiency and exquisite stereoselectivity, how these features are achieved for a non-natural reaction has remained unclear. In this work, the structural determinants responsible for chiral induction and high stereocontrol in Mb(H64V,V68A)-catalyzed cyclopropanation were investigated via a combination of crystallographic, computational (DFT), and structure-activity analyses. Our results show the importance of steric complementarity and non-covalent interactions involving first-sphere active site residues, heme-carbene, and the olefin substrate, in dictating the stereochemical outcome of the cyclopropanation reaction. High stereocontrol is achieved through two major mechanisms. First, by enforcing a specific conformation of the heme-bound carbene within the active site. Second, by controlling the geometry of attack of the olefin on the carbene via steric occlusion, attractive van der Waals forces and protein-mediated pi-pi interactions with the olefin substrate. These insights could be leveraged to expand the substrate scope of the myoglobin-based cyclopropanation catalyst toward non-activated olefins and to increase its cyclopropanation activity in the presence of a bulky alpha-diazo-ester. This work sheds first light into the origin of enzyme-catalyzed enantioselective cyclopropanation, furnishing a mechanistic framework for both understanding the reactivity of current systems and guiding the future development of biological catalysts for this class of synthetically important, abiotic transformations.
-Authors: Bacik, J.P., Ando, N., Fasan, R.
+Origin of high stereocontrol in olefin cyclopropanation catalyzed by an engineered carbene transferase.,Tinoco A, Wei Y, Bacik JP, Carminati DM, Moore EJ, Ando N, Zhang Y, Fasan R ACS Catal. 2019 Feb 1;9(2):1514-1524. doi: 10.1021/acscatal.8b04073. Epub 2018, Dec 28. PMID:31134138<ref>PMID:31134138</ref>
-Description: Engineered sperm whale myoglobin-based carbene transferase
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Bacik, J.P]]
+<div class="pdbe-citations 6m8f" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Pepsin|Pepsin]]
+*[[Proteinase|Proteinase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Phymc]]
+[[Category: Ando, N]]
+[[Category: Bacik, J P]]
 [[Category: Fasan, R]]
-[[Category: Ando, N]]
+[[Category: Carbene transferase]]
+[[Category: Cyclopropanation]]
+[[Category: Heme]]
+[[Category: Metalloprotein]]
+[[Category: Myoglobin]]
+[[Category: Transferase]]