1nox: Difference between revisions

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<StructureSection load='1nox' size='340' side='right'caption='[[1nox]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
<StructureSection load='1nox' size='340' side='right'caption='[[1nox]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1nox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NOX FirstGlance]. <br>
<table><tr><td colspan='2'>[[1nox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NOX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 1.59&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NADH_dehydrogenase NADH dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.3 1.6.99.3] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=1nox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nox OCA], [https://pdbe.org/1nox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nox RCSB], [https://www.ebi.ac.uk/pdbsum/1nox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nox 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=1nox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nox OCA], [https://pdbe.org/1nox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nox RCSB], [https://www.ebi.ac.uk/pdbsum/1nox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nox ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/NOX_THET8 NOX_THET8]] Can oxidize either NADH or NADPH with a preference for NADH. Can catalyze electron transfer from NADH to various electron acceptors which include, in addition to molecular oxygen, cytochrome c, 2,6 dichlorphenolindophenol, methylene blue, ferricyanide or P-nitroblue tetrazolium.  
[https://www.uniprot.org/uniprot/NOX_THET8 NOX_THET8] Can oxidize either NADH or NADPH with a preference for NADH. Can catalyze electron transfer from NADH to various electron acceptors which include, in addition to molecular oxygen, cytochrome c, 2,6 dichlorphenolindophenol, methylene blue, ferricyanide or P-nitroblue tetrazolium.
== 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=1nox 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=1nox ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structures of the flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) containing isoforms of NADH oxidase from Thermus thermophilus have been determined by isomorphous and molecular replacement and refined to 2.3 A and 1.6 A resolution with R-values of 18.5% and 18.6% respectively. The structure of the homodimeric enzyme consists of a central 4-stranded antiparallel beta-sheet covered by helices, a more flexible domain formed by two helices, and a C-terminal excursion connecting the subunits. The active sites are located in a deep cleft between the subunits. The binding site of the flavin cofactor lacks the common nucleotide binding fold and is different from the FMN binding site found in flavodoxins.
Crystal structure of NADH oxidase from Thermus thermophilus.,Hecht HJ, Erdmann H, Park HJ, Sprinzl M, Schmid RD Nat Struct Biol. 1995 Dec;2(12):1109-14. PMID:8846223<ref>PMID:8846223</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1nox" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: NADH dehydrogenase]]
[[Category: Thermus thermophilus HB8]]
[[Category: Thet8]]
[[Category: Erdmann H]]
[[Category: Erdmann, H]]
[[Category: Hecht HJ]]
[[Category: Hecht, H J]]
[[Category: Park HJ]]
[[Category: Park, H J]]
[[Category: Schmid RD]]
[[Category: Schmid, R D]]
[[Category: Sprinzl M]]
[[Category: Sprinzl, M]]
[[Category: Flavoenzyme]]
[[Category: Flavoprotein fmn]]
[[Category: Oxidoreductase]]
[[Category: Thermophile]]

Latest revision as of 07:58, 14 February 2024

NADH OXIDASE FROM THERMUS THERMOPHILUS

1nox, resolution 1.59Å

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