3lsi: Difference between revisions

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<StructureSection load='3lsi' size='340' side='right'caption='[[3lsi]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3lsi' size='340' side='right'caption='[[3lsi]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3lsi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Coriolus_zonatus Coriolus zonatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LSI FirstGlance]. <br>
<table><tr><td colspan='2'>[[3lsi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trametes_ochracea Trametes ochracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LSI FirstGlance]. <br>
</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></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]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3lsh|3lsh]], [[3lsk|3lsk]], [[3lsm|3lsm]]</div></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></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">p2o ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=230624 Coriolus zonatus])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pyranose_oxidase Pyranose oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.10 1.1.3.10] </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=3lsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsi OCA], [https://pdbe.org/3lsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lsi RCSB], [https://www.ebi.ac.uk/pdbsum/3lsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lsi 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=3lsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsi OCA], [https://pdbe.org/3lsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lsi RCSB], [https://www.ebi.ac.uk/pdbsum/3lsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lsi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7ZA32_TRAOC Q7ZA32_TRAOC]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lsi ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lsi ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Flavoenzymes perform a wide range of redox reactions in nature, and a subclass of flavoenzymes carry covalently bound cofactor. The enzyme-flavin bond helps to increase the flavin's redox potential to facilitate substrate oxidation in several oxidases. The formation of the enzyme-flavin covalent bond--the flavinylation reaction--has been studied for the past 40 years. For the most advocated mechanism of autocatalytic flavinylation, the quinone methide mechanism, appropriate stabilization of developing negative charges at the flavin N(1) and N(5) loci is crucial. Whereas the structural basis for stabilization at N(1) is relatively well studied, the structural requisites for charge stabilization at N(5) remain less clear. Here, we show that flavinylation of histidine 167 of pyranose 2-oxidase from Trametes multicolor requires hydrogen bonding at the flavin N(5)/O(4) locus, which is offered by the side chain of Thr169 when the enzyme is in its closed, but not open, state. Moreover, our data show that additional stabilization at N(5) by histidine 548 is required to ensure high occupancy of the histidyl-flavin bond. The combination of structural and spectral data on pyranose 2-oxidase mutants supports the quinone methide mechanism. Our results demonstrate an elaborate structural fine-tuning of the active site to complete its own formation that couples efficient holoenzyme synthesis to conformational substates of the substrate-recognition loop and concerted movements of side chains near the flavinylation ligand.
H-bonding and positive charge at the N5/O4 locus are critical for covalent flavin attachment in trametes pyranose 2-oxidase.,Tan TC, Pitsawong W, Wongnate T, Spadiut O, Haltrich D, Chaiyen P, Divne C J Mol Biol. 2010 Sep 24;402(3):578-94. Epub 2010 Aug 12. PMID:20708626<ref>PMID:20708626</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3lsi" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Pyranose oxidase|Pyranose oxidase]]
*[[Pyranose oxidase|Pyranose oxidase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Coriolus zonatus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pyranose oxidase]]
[[Category: Trametes ochracea]]
[[Category: Divne, C]]
[[Category: Divne C]]
[[Category: Spadiut, O]]
[[Category: Spadiut O]]
[[Category: Tan, T C]]
[[Category: Tan TC]]
[[Category: Gmc oxidoreductase]]
[[Category: Homotetramer]]
[[Category: Non-covalent fad]]
[[Category: Oxidoreductase]]
[[Category: Phbh fold]]
[[Category: Rossmann fold]]
[[Category: T169a mutant]]

Latest revision as of 13:22, 21 February 2024

Pyranose 2-oxidase T169A, tetragonalPyranose 2-oxidase T169A, tetragonal

Structural highlights

3lsi is a 2 chain structure with sequence from Trametes ochracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q7ZA32_TRAOC

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3lsi, resolution 1.90Å

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OCA
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