1hnc: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1hnc.jpg|left|200px]] | [[Image:1hnc.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1hnc", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1hnc| PDB=1hnc | SCENE= }} | ||
}} | |||
'''CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY''' | '''CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY''' | ||
| Line 32: | Line 29: | ||
[[Category: Raghunathan, S.]] | [[Category: Raghunathan, S.]] | ||
[[Category: Rule, G S.]] | [[Category: Rule, G S.]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:02:13 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 19:02, 2 May 2008
CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY
OverviewOverview
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.
About this StructureAbout this Structure
1HNC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 19:02:13 2008