1mtc: Difference between revisions

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[[Image:1mtc.jpg|left|200px]]


<!--
==GLUTATHIONE TRANSFERASE MUTANT Y115F==
The line below this paragraph, containing "STRUCTURE_1mtc", creates the "Structure Box" on the page.
<StructureSection load='1mtc' size='340' side='right'caption='[[1mtc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1mtc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MTC FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene></td></tr>
{{STRUCTURE_1mtc| PDB=1mtc |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mtc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mtc OCA], [https://pdbe.org/1mtc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mtc RCSB], [https://www.ebi.ac.uk/pdbsum/1mtc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mtc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.
== 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/mt/1mtc_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=1mtc ConSurf].
<div style="clear:both"></div>


'''GLUTATHIONE TRANSFERASE MUTANT Y115F'''
==See Also==
 
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Glutathione transferase rGSTM1-1 catalyzes the addition of glutathione (GSH) to 1-chloro-2,4-dinitrobenzene, a reaction in which the chemical step is 60-fold faster than the physical step of product release. The hydroxyl group of Y115, located in the active site access channel, controls the egress of product from the active site. The Y115F mutant enzyme has a k(cat) (72 s(-)(1)) that is 3.6-fold larger than that of the native enzyme (20 s(-)(1)). Crystallographic observations and evidence from amide proton exchange kinetics are consistent with localized increases in the degree of segmental motion of the Y115F mutant that are coupled to the enhanced rate of product release. The loss of hydrogen bonding interactions involving the hydroxyl group of Y115 is reflected in subtle alterations in the backbone position, an increase in B-factors for structural elements that comprise the channel to the active site, and, most dramatically, a loss of well-defined electron density near the site of mutation. The kinetics of amide proton exchange are also enhanced by a factor between 3 and 12 in these regions, providing direct, quantitative evidence for changes in local protein dynamics affecting product release. The enhanced product release rate is proposed to derive from a small shift in the equilibrium population of protein conformers that permit egress of the product from the active site.
[[Category: Large Structures]]
 
==About this Structure==
1MTC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MTC OCA].
 
==Reference==
Local protein dynamics and catalysis: detection of segmental motion associated with rate-limiting product release by a glutathione transferase., Codreanu SG, Ladner JE, Xiao G, Stourman NV, Hachey DL, Gilliland GL, Armstrong RN, Biochemistry. 2002 Dec 24;41(51):15161-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12484753 12484753]
[[Category: Glutathione transferase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Armstrong RN]]
[[Category: Armstrong, R N.]]
[[Category: Gilliland GL]]
[[Category: Gilliland, G L.]]
[[Category: Ladner JE]]
[[Category: Ladner, J E.]]
[[Category: Xiao G]]
[[Category: Xiao, G.]]
[[Category: Glutathione transferase]]
[[Category: Protein catalysis]]
[[Category: Protein dynamic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:41:47 2008''

Latest revision as of 07:48, 14 February 2024

GLUTATHIONE TRANSFERASE MUTANT Y115F

1mtc, resolution 2.20Å

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