1kte

From Proteopedia

(Difference between revisions)

Current revision

CRYSTAL STRUCTURE OF THIOLTRANSFERASE AT 2.2 ANGSTROM RESOLUTION

Structural highlights

1kte is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLRX1_PIG Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.

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

We report here the first three-dimensional structure of a mammalian thioltransferase as determined by single crystal X-ray crystallography at 2.2 A resolution. The protein is known for its thiol-redox properties and dehydroascorbate reductase activity. Recombinant pig liver thioltransferase expressed in Escherichia coli was crystallized in its oxidized form by vapor diffusion technique. The structure was determined by multiple isomorphous replacement method using four heavy-atom derivatives. The protein folds into an alpha/beta structure with a four-stranded mixed beta-sheet in the core, flanked on either side by helices. The fold is similar to that found in other thiol-redox proteins, viz. E. coli thioredoxin and bacteriophage T4 glutaredoxin, and thus seems to be conserved in these functionally related proteins. The active site disulfide (Cys 22-Cys 25) is located on a protrusion on the molecular surface. Cys 22, which is known to have an abnormally low pKa of 3.8, is accessible from the exterior of the molecule. Pro 70, which is in close proximity to the disulfide bridge, assumes a conserved cis-peptide configuration. Mutational data available on the protein are in agreement with the three-dimensional structure.

Crystal structure of thioltransferase at 2.2 A resolution.,Katti SK, Robbins AH, Yang Y, Wells WW Protein Sci. 1995 Oct;4(10):1998-2005. PMID:8535236^[1]

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

References

↑ Katti SK, Robbins AH, Yang Y, Wells WW. Crystal structure of thioltransferase at 2.2 A resolution. Protein Sci. 1995 Oct;4(10):1998-2005. PMID:8535236

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/1kte"

Categories: Large Structures | Sus scrofa | Katti SK | Robbins AH

@@ Line 3: / Line 3: @@
 <StructureSection load='1kte' size='340' side='right'caption='[[1kte]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kte]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KTE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kte]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KTE FirstGlance]. <br>
-</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=1kte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kte OCA], [https://pdbe.org/1kte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kte RCSB], [https://www.ebi.ac.uk/pdbsum/1kte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kte ProSAT]</span></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]] 2.2&#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=1kte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kte OCA], [https://pdbe.org/1kte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kte RCSB], [https://www.ebi.ac.uk/pdbsum/1kte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kte ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GLRX1_PIG GLRX1_PIG]] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
+[https://www.uniprot.org/uniprot/GLRX1_PIG GLRX1_PIG] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 13: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kt/1kte_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 32: / Line 33: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Pig]]
+[[Category: Sus scrofa]]
-[[Category: Katti, S K]]
+[[Category: Katti SK]]
-[[Category: Robbins, A H]]
+[[Category: Robbins AH]]
-[[Category: Acetylation]]
-[[Category: Electron transport]]
-[[Category: Redox-active center]]

1kte

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF THIOLTRANSFERASE AT 2.2 ANGSTROM RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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