6fow: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure.==
==The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure.==
<StructureSection load='6fow' size='340' side='right' caption='[[6fow]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
<StructureSection load='6fow' size='340' side='right'caption='[[6fow]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6fow]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/'streptomyces_maritimus' 'streptomyces maritimus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FOW FirstGlance]. <br>
<table><tr><td colspan='2'>[[6fow]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_maritimus Streptomyces maritimus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FOW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">encM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=115828 'Streptomyces maritimus'])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></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=6fow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fow OCA], [http://pdbe.org/6fow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fow RCSB], [http://www.ebi.ac.uk/pdbsum/6fow PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fow ProSAT]</span></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=6fow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fow OCA], [https://pdbe.org/6fow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fow RCSB], [https://www.ebi.ac.uk/pdbsum/6fow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fow ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q9KHK2_9ACTN Q9KHK2_9ACTN]
The reactions of enzymes and cofactors with gaseous molecules such as dioxygen (O2) are challenging to study and remain among the most contentious subjects in biochemistry. To date, it is largely enigmatic how enzymes control and fine-tune their reactions with O2, as exemplified by the ubiquitous flavin-dependent enzymes that commonly facilitate redox chemistry such as the oxygenation of organic substrates. Here we employ O2-pressurized X-ray crystallography and quantum mechanical calculations to reveal how the precise positioning of O2 within a flavoenzyme's active site enables the regiospecific formation of a covalent flavin-oxygen adduct and oxygenating species (i.e., the flavin-N5-oxide) by mimicking a critical transition state. This study unambiguously demonstrates how enzymes may control the O2 functionalization of an organic cofactor as prerequisite for oxidative catalysis. Our work thus illustrates how O2 reactivity can be harnessed in an enzymatic environment and provides crucial knowledge for future rational design of O2-reactive enzymes.
 
Enzymatic control of dioxygen binding and functionalization of the flavin cofactor.,Saleem-Batcha R, Stull F, Sanders JN, Moore BS, Palfey BA, Houk KN, Teufel R Proc Natl Acad Sci U S A. 2018 Apr 23. pii: 1801189115. doi:, 10.1073/pnas.1801189115. PMID:29686059<ref>PMID:29686059</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fow" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces maritimus]]
[[Category: Streptomyces maritimus]]
[[Category: Saleem-Batcha, R]]
[[Category: Saleem-Batcha R]]
[[Category: Teufel, R]]
[[Category: Teufel R]]
[[Category: Encm]]
[[Category: Fad]]
[[Category: Flavin-n5-oxide]]
[[Category: Flavoprotein]]
[[Category: Monooxygenase]]
[[Category: Oxygen binding]]
[[Category: Oxygenating species]]

Latest revision as of 07:48, 7 February 2024

The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure.

6fow, resolution 2.04Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=6fow&oldid=4045940"