1hnc: Difference between revisions

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-[[Image:1hnc.jpg|left|200px]]<br /><applet load="1hnc" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1hnc, resolution 3.0&Aring;" />
-'''CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY==
-The structures of three crystal forms of the class mu human glutathione, transferase GSTM2-2 have been determined. X-ray phase information was, obtained independently from molecular replacement and from anomalous, scattering by a single isomorphous derivative. One crystal form contains a, single monomer in the asymmetric unit and has been refined to 1.85 A with, an overall R factor of 22.6%. The second form contains a single dimer in, the asymmetric unit and has been refined to 3.5 A with an R factor of, 20.7%. The third form contains two dimers in the asymmetric unit and has, been refined to 3.0 A with an R factor of 25.0%. Although all three, crystal forms were grown from solutions that contained, glutathione-dinitrobenzene, electron density can only be seen for the, glutathione portion of the ligand. The first 202 residues in the seven, crystallographically independent monomers of GSTM2-2 are essentially, identical in structure. However, heterogeneity in the conformation of the, side-chain of Tyr115 is observed in the different monomers. The tertiary, structure of residues 1-202 is similar to that of the corresponding region, in the class mu isoform of glutathione transferase from rat, GST3-3 (Ji et, al. (1992), Biochemistry, 31, 10169-10184). However, significant, differences in the conformation of the two enzymes have been observed in, the region of the active site that binds hydrophobic substrates. These, differences include a 2 A shift in the carboxy terminus of a helix, and, significant heterogeneity in the conformation of the last 15 residues of, the carboxy terminus. The conformation and degree of disorder of the last, 15 residues correlates with the extent of protein-protein contacts within, the unit cell.
+<StructureSection load='1hnc' size='340' side='right'caption='[[1hnc]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1hnc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HNC 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]] 3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDN:GLUTATHIONE+S-(2,4+DINITROBENZENE)'>GDN</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=1hnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnc OCA], [https://pdbe.org/1hnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hnc RCSB], [https://www.ebi.ac.uk/pdbsum/1hnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hnc ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GSTM2_HUMAN GSTM2_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:16549767</ref>
+== 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/hn/1hnc_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=1hnc ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-HNC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GDN:'>GDN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNC OCA].
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
+== References ==
-==Reference==
+<references/>
-Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity., Raghunathan S, Chandross RJ, Kretsinger RH, Allison TJ, Penington CJ, Rule GS, J Mol Biol. 1994 May 20;238(5):815-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8182750 8182750]
+__TOC__
-[[Category: Glutathione transferase]]
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Allison, T.J.]]
+[[Category: Allison TJ]]
-[[Category: Chandross, R.J.]]
+[[Category: Chandross RJ]]
-[[Category: Kretsinger, R.H.]]
+[[Category: Kretsinger RH]]
-[[Category: Penington, C.J.]]
+[[Category: Penington CJ]]
-[[Category: Raghunathan, S.]]
+[[Category: Raghunathan S]]
-[[Category: Rule, G.S.]]
+[[Category: Rule GS]]
-[[Category: GDN]]
-[[Category: transferase(glutathione)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:57:15 2008''