1nox

From Proteopedia

(Difference between revisions)

Revision as of 07:05, 25 August 2021

NADH OXIDASE FROM THERMUS THERMOPHILUS

Structural highlights

1nox is a 1 chain structure with sequence from Thet8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	NADH dehydrogenase, with EC number 1.6.99.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

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

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hecht HJ, Erdmann H, Park HJ, Sprinzl M, Schmid RD. Crystal structure of NADH oxidase from Thermus thermophilus. Nat Struct Biol. 1995 Dec;2(12):1109-14. PMID:8846223

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nox"

@@ Line 3: / Line 3: @@
 <StructureSection load='1nox' size='340' side='right'caption='[[1nox]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1nox]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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/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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
+</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADH_dehydrogenase NADH dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.3 1.6.99.3] </span></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='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=1nox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nox OCA], [http://pdbe.org/1nox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nox RCSB], [http://www.ebi.ac.uk/pdbsum/1nox PDBsum], [http://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>
 == Function ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1nox

From Proteopedia

Revision as of 07:05, 25 August 2021

NADH OXIDASE FROM THERMUS THERMOPHILUS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox