1wou

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of human Trp14

Structural highlights

1wou is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TXD17_HUMAN Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.^[1] ^[2]

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-related protein 14 (TRP14) is involved in regulating tumor necrosis factor-alpha-induced signaling pathways in a different manner from human thioredoxin 1 (Trx1). Here, we report the crystal structure of human TRP14 determined at 1.8-A resolutions. The structure reveals a typical thioredoxin fold with characteristic structural features that account for the substrate specificity of the protein. The surface of TRP14 in the vicinity of the active site includes an extended loop and an additional alpha-helix, and the distribution of charged residues in the surface is different from Trx1. The distinctive dipeptide between the redox-active cysteines contributes to stabilizing the thiolate anion of the active site cysteine 43, increasing reactivity of the cysteine toward substrates. These structural differences in the active site suggest that TRP14 has evolved to regulate cellular redox signaling by recognizing a distinctive group of substrates that would complement the group of proteins regulated by Trx1.

Structural basis of cellular redox regulation by human TRP14.,Woo JR, Kim SJ, Jeong W, Cho YH, Lee SC, Chung YJ, Rhee SG, Ryu SE J Biol Chem. 2004 Nov 12;279(46):48120-5. Epub 2004 Sep 7. PMID:15355959^[3]

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

References

↑ Jeong W, Yoon HW, Lee SR, Rhee SG. Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa. New insights into the specificity of thioredoxin function. J Biol Chem. 2004 Jan 30;279(5):3142-50. Epub 2003 Nov 7. PMID:14607844 doi:http://dx.doi.org/10.1074/jbc.M307932200
↑ Jeong W, Chang TS, Boja ES, Fales HM, Rhee SG. Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways. J Biol Chem. 2004 Jan 30;279(5):3151-9. Epub 2003 Nov 7. PMID:14607843 doi:http://dx.doi.org/10.1074/jbc.M307959200
↑ Woo JR, Kim SJ, Jeong W, Cho YH, Lee SC, Chung YJ, Rhee SG, Ryu SE. Structural basis of cellular redox regulation by human TRP14. J Biol Chem. 2004 Nov 12;279(46):48120-5. Epub 2004 Sep 7. PMID:15355959 doi:10.1074/jbc.M407079200

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/1wou"

@@ Line 1: / Line 1: @@
-[[Image:1wou.gif|left|200px]]<br />
-<applet load="1wou" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1wou, resolution 1.8&Aring;" />
-'''Crystal Structure of human Trp14'''<br />
-==Overview==
+==Crystal Structure of human Trp14==
-Thioredoxin-related protein 14 (TRP14) is involved in regulating tumor, necrosis factor-alpha-induced signaling pathways in a different manner, from human thioredoxin 1 (Trx1). Here, we report the crystal structure of, human TRP14 determined at 1.8-A resolutions. The structure reveals a, typical thioredoxin fold with characteristic structural features that, account for the substrate specificity of the protein. The surface of TRP14, in the vicinity of the active site includes an extended loop and an, additional alpha-helix, and the distribution of charged residues in the, surface is different from Trx1. The distinctive dipeptide between the, redox-active cysteines contributes to stabilizing the thiolate anion of, the active site cysteine 43, increasing reactivity of the cysteine toward, substrates. These structural differences in the active site suggest that, TRP14 has evolved to regulate cellular redox signaling by recognizing a, distinctive group of substrates that would complement the group of, proteins regulated by Trx1.
+<StructureSection load='1wou' size='340' side='right'caption='[[1wou]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1wou]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WOU FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1wou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wou OCA], [https://pdbe.org/1wou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wou RCSB], [https://www.ebi.ac.uk/pdbsum/1wou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wou ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TXD17_HUMAN TXD17_HUMAN] Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.<ref>PMID:14607844</ref> <ref>PMID:14607843</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wo/1wou_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1wou ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Thioredoxin-related protein 14 (TRP14) is involved in regulating tumor necrosis factor-alpha-induced signaling pathways in a different manner from human thioredoxin 1 (Trx1). Here, we report the crystal structure of human TRP14 determined at 1.8-A resolutions. The structure reveals a typical thioredoxin fold with characteristic structural features that account for the substrate specificity of the protein. The surface of TRP14 in the vicinity of the active site includes an extended loop and an additional alpha-helix, and the distribution of charged residues in the surface is different from Trx1. The distinctive dipeptide between the redox-active cysteines contributes to stabilizing the thiolate anion of the active site cysteine 43, increasing reactivity of the cysteine toward substrates. These structural differences in the active site suggest that TRP14 has evolved to regulate cellular redox signaling by recognizing a distinctive group of substrates that would complement the group of proteins regulated by Trx1.
-==About this Structure==
+Structural basis of cellular redox regulation by human TRP14.,Woo JR, Kim SJ, Jeong W, Cho YH, Lee SC, Chung YJ, Rhee SG, Ryu SE J Biol Chem. 2004 Nov 12;279(46):48120-5. Epub 2004 Sep 7. PMID:15355959<ref>PMID:15355959</ref>
-WOU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WOU OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structural basis of cellular redox regulation by human TRP14., Woo JR, Kim SJ, Jeong W, Cho YH, Lee SC, Chung YJ, Rhee SG, Ryu SE, J Biol Chem. 2004 Nov 12;279(46):48120-5. Epub 2004 Sep 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15355959 15355959]
+</div>
+<div class="pdbe-citations 1wou" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Cho, Y.H.]]
+[[Category: Cho YH]]
-[[Category: Chung, Y.J.]]
+[[Category: Chung YJ]]
-[[Category: Jeong, W.]]
+[[Category: Jeong W]]
-[[Category: Kim, S.J.]]
+[[Category: Kim SJ]]
-[[Category: Lee, S.C.]]
+[[Category: Lee SC]]
-[[Category: Rhee, S.G.]]
+[[Category: Rhee SG]]
-[[Category: Ryu, S.E.]]
+[[Category: Ryu SE]]
-[[Category: Woo, J.R.]]
+[[Category: Woo JR]]
-[[Category: electron transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:53:08 2007''

1wou

From Proteopedia

Current revision

Crystal Structure of human Trp14

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