This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1aaz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1aaz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aaz, resolution 2.0&Aring;" /> '''THE STRUCTURE OF OXID...)
Current revision (15:22, 13 March 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1aaz.gif|left|200px]]<br /><applet load="1aaz" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1aaz, resolution 2.0&Aring;" />
 
-
'''THE STRUCTURE OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXIN (THIOREDOXIN)'''<br />
 
-
==Overview==
+
==THE STRUCTURE OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXIN (THIOREDOXIN)==
-
The structure of wild-type bacteriophage T4 glutaredoxin (earlier called, thioredoxin) in its oxidized form has been refined in a monoclinic crystal, form at 2.0 A resolution to a crystallographic R-factor of 0.209. A mutant, T4 glutaredoxin gives orthorhombic crystals of better quality. The, structure of this mutant has been solved by molecular replacement methods, and refined at 1.45 A to an R-value of 0.175. In this mutant glutaredoxin, the active site residues Val15 and Tyr16 have been substituted by Gly and, Pro, respectively, to mimic that of Escherichia coli thioredoxin. The, main-chain conformation of the wild-type protein is similar in the two, independently determined molecules in the asymmetric unit of the, monoclinic crystals. On the other hand, side-chain conformations differ, considerably between the two molecules due to heterologous packing, interactions in the crystals. The structure of the mutant protein is very, similar to the wild-type protein, except at mutated positions and at parts, involved in crystal contacts. The active site disulfide bridge between, Cys14 and Cys17 is located at the first turn of helix alpha 1. The torsion, angles of these residues are similar to those of Escherichia coli, thioredoxin. The torsion angle around the S-S bond is smaller than that, normally observed for disulfides: 58 degrees, 67 degrees and 67 degrees, for wild-type glutaredoxin molecule A and B and mutant glutaredoxin, respectively. Each sulfur atom of the disulfide cysteines in T4, glutaredoxin forms a hydrogen bond to one main-chain nitrogen atom. The, active site is shielded from solvent on one side by the beta-carbon atoms, of the cysteine residues plus side-chains of residues 7, 9, 21 and 33., From the opposite side, there is a cleft where the sulfur atom of Cys14 is, accessible and can be attacked by a nucleophilic thiolate ion in the, initial step of the reduction reaction.
+
<StructureSection load='1aaz' size='340' side='right'caption='[[1aaz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1aaz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AAZ FirstGlance]. <br>
-
1AAZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AAZ OCA].
+
</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&#8491;</td></tr>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aaz OCA], [https://pdbe.org/1aaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aaz RCSB], [https://www.ebi.ac.uk/pdbsum/1aaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aaz ProSAT]</span></td></tr>
-
Structure of oxidized bacteriophage T4 glutaredoxin (thioredoxin). Refinement of native and mutant proteins., Eklund H, Ingelman M, Soderberg BO, Uhlin T, Nordlund P, Nikkola M, Sonnerstam U, Joelson T, Petratos K, J Mol Biol. 1992 Nov 20;228(2):596-618. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1453466 1453466]
+
</table>
-
[[Category: Bacteriophage t4]]
+
== Function ==
-
[[Category: Single protein]]
+
[https://www.uniprot.org/uniprot/GLRX_BPT4 GLRX_BPT4] Serves as a reducing agent for the phage-induced ribonucleotide reductase, but not for the bacterial ones. This specificity may be the result of sequence differences around the redox-active disulfide bond. The oxidized form accepts electrons from bacterial glutathione and will, in turn, reduce other small disulfides. Can also be reduced by NADPH and by bacterial thioredoxin reductase.<ref>PMID:8440680</ref>
-
[[Category: Eklund, H.]]
+
== Evolutionary Conservation ==
-
[[Category: Ingelman, M.]]
+
[[Image:Consurf_key_small.gif|200px|right]]
-
[[Category: Joelson, T.]]
+
Check<jmol>
-
[[Category: Nikkola, M.]]
+
<jmolCheckbox>
-
[[Category: Nordlund, P.]]
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/1aaz_consurf.spt"</scriptWhenChecked>
-
[[Category: Petratos, K.]]
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
[[Category: Soderberg, B.O.]]
+
<text>to colour the structure by Evolutionary Conservation</text>
-
[[Category: Sonnerstam, U.]]
+
</jmolCheckbox>
-
[[Category: Uhlin, T.]]
+
</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=1aaz ConSurf].
-
[[Category: CD]]
+
<div style="clear:both"></div>
-
[[Category: electron transport]]
+
== References ==
-
 
+
<references/>
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:43:39 2007''
+
__TOC__
 +
</StructureSection>
 +
[[Category: Escherichia virus T4]]
 +
[[Category: Large Structures]]
 +
[[Category: Eklund H]]
 +
[[Category: Ingelman M]]
 +
[[Category: Joelson T]]
 +
[[Category: Nikkola M]]
 +
[[Category: Nordlund P]]
 +
[[Category: Petratos K]]
 +
[[Category: Soderberg B-O]]
 +
[[Category: Sonnerstam U]]
 +
[[Category: Uhlin T]]

Current revision

THE STRUCTURE OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXIN (THIOREDOXIN)

PDB ID 1aaz

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1aaz"
Personal tools