1hnc: Difference between revisions

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<StructureSection load='1hnc' size='340' side='right'caption='[[1hnc]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1hnc' size='340' side='right'caption='[[1hnc]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1hnc]] is a 4 chain structure. 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>
<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='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>
</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></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>
<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>
</table>
== Function ==
== 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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:8182750<ref>PMID:8182750</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1hnc" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glutathione transferase]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[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]]

Latest revision as of 10:28, 7 February 2024

CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITYCRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY

Structural highlights

1hnc is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GSTM2_HUMAN Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Norrgard MA, Ivarsson Y, Tars K, Mannervik B. Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution. Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):4876-81. Epub 2006 Mar 20. PMID:16549767

1hnc, resolution 3.00Å

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