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New page: left|200px<br /><applet load="1fb0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fb0, resolution 2.26Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1fb0.gif|left|200px]]<br /><applet load="1fb0" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fb0, resolution 2.26&Aring;" />
'''CRYSTAL STRUCTURE OF THIOREDOXIN M FROM SPINACH CHLOROPLAST (REDUCED FORM)'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THIOREDOXIN M FROM SPINACH CHLOROPLAST (REDUCED FORM)==
Thioredoxins are small ubiquitous proteins which act as general protein, disulfide reductases in living cells. Chloroplasts contain two distinct, thioredoxins ( f and m) with different phylogenetic origin. Both act as, enzyme regulatory proteins but have different specificities towards target, enzymes. Thioredoxin f (Trx f), which shares only low sequence identity, with thioredoxin m (Trx m) and with all other known thioredoxins, activates enzymes of the Calvin cycle and other photosynthetic processes., Trx m shows high sequence similarity with bacterial thioredoxins and, activates other chloroplast enzymes. The here described structural studies, of the two chloroplast thioredoxins were carried out in order to gain, insight into the structure/function relationships of these proteins., Crystal structures were determined for oxidized, recombinant thioredoxin f, (Trx f-L) and at the N terminus truncated form of it (Trx f-S), as well as, for oxidized and reduced thioredoxin m (at 2.1 and 2.3 A resolution, respectively). Whereas thioredoxin f crystallized as a monomer, both, truncated thioredoxin f and thioredoxin m crystallized as non-covalent, dimers. The structures of thioredoxins f and m exhibit the typical, thioredoxin fold consisting of a central twisted five-stranded beta-sheet, surrounded by four alpha-helices. Thioredoxin f contains an additional, alpha-helix at the N terminus and an exposed third cysteine close to the, active site. The overall three-dimensional structures of the two, chloroplast thioredoxins are quite similar. However, the two proteins have, a significantly different surface topology and charge distribution around, the active site. An interesting feature which might significantly, contribute to the specificity of thioredoxin f is an inherent flexibility, of its active site, which has expressed itself crystallographically in two, different crystal forms.
<StructureSection load='1fb0' size='340' side='right'caption='[[1fb0]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fb0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FB0 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]] 2.26&#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=1fb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fb0 OCA], [https://pdbe.org/1fb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fb0 RCSB], [https://www.ebi.ac.uk/pdbsum/1fb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fb0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRXM_SPIOL TRXM_SPIOL] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase.
== 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/fb/1fb0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1fb0 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FB0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FB0 OCA].
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structures of two functionally different thioredoxins in spinach chloroplasts., Capitani G, Markovic-Housley Z, DelVal G, Morris M, Jansonius JN, Schurmann P, J Mol Biol. 2000 Sep 8;302(1):135-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10964566 10964566]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
[[Category: Capitani, G.]]
[[Category: Capitani G]]
[[Category: DelVal, G.]]
[[Category: DelVal G]]
[[Category: Jansonius, J.N.]]
[[Category: Jansonius JN]]
[[Category: Markovic-Housley, Z.]]
[[Category: Markovic-Housley Z]]
[[Category: Morris, M.]]
[[Category: Morris M]]
[[Category: Schurmann, P.]]
[[Category: Schurmann P]]
[[Category: electron transport]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:46:47 2007''
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