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[[Image:1jcm.gif|left|200px]]
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{{STRUCTURE_1jcm|  PDB=1jcm  |  SCENE=  }}
'''TRPC STABILITY MUTANT CONTAINING AN ENGINEERED DISULPHIDE BRIDGE AND IN COMPLEX WITH A CDRP-RELATED SUBSTRATE'''


==TRPC STABILITY MUTANT CONTAINING AN ENGINEERED DISULPHIDE BRIDGE AND IN COMPLEX WITH A CDRP-RELATED SUBSTRATE==
<StructureSection load='1jcm' size='340' side='right'caption='[[1jcm]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jcm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JCM 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=137:1-(O-CARBOXY-PHENYLAMINO)-1-DEOXY-D-RIBULOSE-5-PHOSPHATE'>137</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1jcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jcm OCA], [https://pdbe.org/1jcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jcm RCSB], [https://www.ebi.ac.uk/pdbsum/1jcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jcm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRPC_ECOLI TRPC_ECOLI] Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain.
== 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/jc/1jcm_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=1jcm ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The aim of this study was to increase the stability of the thermolabile (betaalpha)8-barrel enzyme indoleglycerol phosphate synthase from Escherichia coli by the introduction of disulfide bridges. For the design of such variants, we selected two out of 12 candidates, in which newly introduced cysteines potentially form optimal disulfide bonds. These variants avoid short-range connections, substitutions near catalytic residues, and crosslinks between the new and the three parental cysteines. The variant linking residues 3 and 189 fastens the N-terminus to the (betaalpha)8-barrel. The rate of thermal inactivation at 50 degrees C of this variant with a closed disulfide bridge is 65-fold slower than that of the reference dithiol form, but only 13-fold slower than that of the parental protein. The near-ultraviolet CD spectrum, the reactivity of parental buried cysteines with Ellman's reagent as well as the decreased turnover number indicate that the protein structure is rigidified. To confirm these data, we have solved the X-ray structure to 2.1-A resolution. The second variant was designed to crosslink the terminal modules betaalpha1 and betaalpha8. However, not even the dithiol form acquired the native fold, possibly because one of the targeted residues is solvent-inaccessible in the parental protein.


==Overview==
Stabilization of a (betaalpha)8-barrel protein by an engineered disulfide bridge.,Ivens A, Mayans O, Szadkowski H, Jurgens C, Wilmanns M, Kirschner K Eur J Biochem. 2002 Feb;269(4):1145-53. PMID:11856350<ref>PMID:11856350</ref>
The aim of this study was to increase the stability of the thermolabile (betaalpha)8-barrel enzyme indoleglycerol phosphate synthase from Escherichia coli by the introduction of disulfide bridges. For the design of such variants, we selected two out of 12 candidates, in which newly introduced cysteines potentially form optimal disulfide bonds. These variants avoid short-range connections, substitutions near catalytic residues, and crosslinks between the new and the three parental cysteines. The variant linking residues 3 and 189 fastens the N-terminus to the (betaalpha)8-barrel. The rate of thermal inactivation at 50 degrees C of this variant with a closed disulfide bridge is 65-fold slower than that of the reference dithiol form, but only 13-fold slower than that of the parental protein. The near-ultraviolet CD spectrum, the reactivity of parental buried cysteines with Ellman's reagent as well as the decreased turnover number indicate that the protein structure is rigidified. To confirm these data, we have solved the X-ray structure to 2.1-A resolution. The second variant was designed to crosslink the terminal modules betaalpha1 and betaalpha8. However, not even the dithiol form acquired the native fold, possibly because one of the targeted residues is solvent-inaccessible in the parental protein.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1JCM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JCM OCA].
</div>
<div class="pdbe-citations 1jcm" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Stabilization of a (betaalpha)8-barrel protein by an engineered disulfide bridge., Ivens A, Mayans O, Szadkowski H, Jurgens C, Wilmanns M, Kirschner K, Eur J Biochem. 2002 Feb;269(4):1145-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11856350 11856350]
*[[IGPS 3D structures|IGPS 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Indole-3-glycerol-phosphate synthase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Ivens A]]
[[Category: Ivens, A.]]
[[Category: Kirschner K]]
[[Category: Kirschner, K.]]
[[Category: Mayans O]]
[[Category: Mayans, O.]]
[[Category: Szadkowski H]]
[[Category: Szadkowski, H.]]
[[Category: Wilmanns M]]
[[Category: Wilmanns, M.]]
[[Category: Beta-alpha-barrel]]
[[Category: Disulphide bridge]]
[[Category: Stability mutant]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:03:40 2008''
Retrieved from "https://proteopedia.org/1jcm"