6fuu: Difference between revisions
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New page: '''Unreleased structure''' The entry 6fuu is ON HOLD Authors: Reddem, E.R., Thunnissen, A.M.W.H. Description: Transcriptional regulator LmrR with bound heme [[Category: Unreleased Stru... |
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The | ==Transcriptional regulator LmrR with bound heme== | ||
<StructureSection load='6fuu' size='340' side='right' caption='[[6fuu]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fuu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptococcus_hollandicus"_scholl_1891 "streptococcus hollandicus" scholl 1891]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FUU 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></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NCDO763_1045, VN96_2738 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1359 "Streptococcus hollandicus" Scholl 1891])</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=6fuu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fuu OCA], [http://pdbe.org/6fuu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fuu RCSB], [http://www.ebi.ac.uk/pdbsum/6fuu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fuu ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
An artificial heme enzyme was created by self-assembly from hemin and the Lactococcal multidrug resistance Regulator (LmrR). The crystal structure shows the heme bound inside the hydrophobic pore of the protein, where it appears inaccessible for substrates. Yet, good catalytic activity and moderate enantioselectivity was observed in the abiological cyclopropanation reaction. We proposed that the dynamic nature of the structure of the LmrR protein is key to the observed activity. This was supported by molecular dynamics simulations, which showed transient formation of opened conformations allowing for binding of substrates and formation of pre-catalytic structures. | |||
An Artificial Heme Enzyme for Cyclopropanation Reactions.,Villarino L, Splan K, Reddem E, Gutierrez de Souza C, Alonso-Cotchico L, Lledos A, Marechal JD, Thunnissen AM, Roelfes G Angew Chem Int Ed Engl. 2018 May 2. doi: 10.1002/anie.201802946. PMID:29719099<ref>PMID:29719099</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Thunnissen, A | <div class="pdbe-citations 6fuu" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Streptococcus hollandicus scholl 1891]] | |||
[[Category: Reddem, E R]] | |||
[[Category: Thunnissen, A M.W H]] | |||
[[Category: Artificial enzyme]] | |||
[[Category: Complex]] | |||
[[Category: Dna binding protein]] | |||
[[Category: Heme-based catalysis]] | |||
[[Category: Multi-drug resistance]] | |||
[[Category: Transcriptional regulator]] | |||
Latest revision as of 08:59, 27 June 2018
Transcriptional regulator LmrR with bound hemeTranscriptional regulator LmrR with bound heme
Structural highlights
Publication Abstract from PubMedAn artificial heme enzyme was created by self-assembly from hemin and the Lactococcal multidrug resistance Regulator (LmrR). The crystal structure shows the heme bound inside the hydrophobic pore of the protein, where it appears inaccessible for substrates. Yet, good catalytic activity and moderate enantioselectivity was observed in the abiological cyclopropanation reaction. We proposed that the dynamic nature of the structure of the LmrR protein is key to the observed activity. This was supported by molecular dynamics simulations, which showed transient formation of opened conformations allowing for binding of substrates and formation of pre-catalytic structures. An Artificial Heme Enzyme for Cyclopropanation Reactions.,Villarino L, Splan K, Reddem E, Gutierrez de Souza C, Alonso-Cotchico L, Lledos A, Marechal JD, Thunnissen AM, Roelfes G Angew Chem Int Ed Engl. 2018 May 2. doi: 10.1002/anie.201802946. PMID:29719099[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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