1zkq

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of mouse thioredoxin reductase type 2

Structural highlights

1zkq is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRXR2_MOUSE Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.

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

Thioredoxin reductase (TrxR) is an essential enzyme required for the efficient maintenance of the cellular redox homeostasis, particularly in cancer cells that are sensitive to reactive oxygen species. In mammals, distinct isozymes function in the cytosol and mitochondria. Through an intricate mechanism, these enzymes transfer reducing equivalents from NADPH to bound FAD and subsequently to an active-site disulfide. In mammalian TrxRs, the dithiol then reduces a mobile C-terminal selenocysteine-containing tetrapeptide of the opposing subunit of the dimer. Once activated, the C-terminal redox center reduces a disulfide bond within thioredoxin. In this report, we present the structural data on a mitochondrial TrxR, TrxR2 (also known as TR3 and TxnRd2). Mouse TrxR2, in which the essential selenocysteine residue had been replaced with cysteine, was isolated as a FAD-containing holoenzyme and crystallized (2.6 A; R = 22.2%; R(free) = 27.6%). The addition of NADPH to the TrxR2 crystals resulted in a color change, indicating reduction of the active-site disulfide and formation of a species presumed to be the flavin-thiolate charge transfer complex. Examination of the NADP(H)-bound model (3.0 A; R = 24.1%; R(free) = 31.2%) indicates that an active-site tyrosine residue must rotate from its initial position to stack against the nicotinamide ring of NADPH, which is juxtaposed to the isoalloxazine ring of FAD to facilitate hydride transfer. Detailed analysis of the structural data in conjunction with a model of the unusual C-terminal selenenylsulfide suggests molecular details of the reaction mechanism and highlights evolutionary adaptations among reductases.

Crystal structures of oxidized and reduced mitochondrial thioredoxin reductase provide molecular details of the reaction mechanism.,Biterova EI, Turanov AA, Gladyshev VN, Barycki JJ Proc Natl Acad Sci U S A. 2005 Oct 18;102(42):15018-23. Epub 2005 Oct 10. PMID:16217027^[1]

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

References

↑ Biterova EI, Turanov AA, Gladyshev VN, Barycki JJ. Crystal structures of oxidized and reduced mitochondrial thioredoxin reductase provide molecular details of the reaction mechanism. Proc Natl Acad Sci U S A. 2005 Oct 18;102(42):15018-23. Epub 2005 Oct 10. PMID:16217027

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1zkq' size='340' side='right'caption='[[1zkq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1zkq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZKQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ZKQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1zkq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZKQ 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]] 2.6&#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;'>[[1zdl|1zdl]], [[1h6v|1h6v]], [[3grs|3grs]]</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">Txnrd2, Trxr2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=1zkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zkq OCA], [https://pdbe.org/1zkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zkq RCSB], [https://www.ebi.ac.uk/pdbsum/1zkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zkq ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1zkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zkq OCA], [http://pdbe.org/1zkq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zkq RCSB], [http://www.ebi.ac.uk/pdbsum/1zkq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zkq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TRXR2_MOUSE TRXR2_MOUSE]] Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.
+[https://www.uniprot.org/uniprot/TRXR2_MOUSE TRXR2_MOUSE] Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 32: @@
 ==See Also==
 *[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]]
-*[[User:Sarah Abdalla/Thioredoxin Reductase|User:Sarah Abdalla/Thioredoxin Reductase]]
 == References ==
 <references/>
@@ Line 40: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Thioredoxin-disulfide reductase]]
+[[Category: Barycki JJ]]
-[[Category: Barycki, J J]]
+[[Category: Biterova EI]]
-[[Category: Biterova, E I]]
+[[Category: Gladyshev VN]]
-[[Category: Gladyshev, V N]]
+[[Category: Turanov AA]]
-[[Category: Turanov, A A]]
-[[Category: Flavoprotein]]
-[[Category: Oxidoreductase]]
-[[Category: Reductase]]
-[[Category: Selenocysteine]]
-[[Category: Thioredoxin]]

1zkq

From Proteopedia

Current revision

Crystal structure of mouse thioredoxin reductase type 2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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