1msd: Difference between revisions

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COMPARISON OF THE CRYSTAL STRUCTURES OF GENETICALLY ENGINEERED HUMAN MANGANESE SUPEROXIDE DISMUTASE AND MANGANESE SUPEROXIDE DISMUTASE FROM THERMUS THERMOPHILUS. DIFFERENCES IN DIMER-DIMER INTERACTIONS.

OverviewOverview

The three-dimensional X-ray structure of a recombinant human mitochondrial manganese superoxide dismutase (MnSOD) (chain length 198 residues) was determined by the method of molecular replacement using the related structure of MnSOD from Thermus thermophilus as a search model. This tetrameric human MnSOD crystallizes in space group P2(1)2(1)2 with a dimer in the asymmetric unit (Wagner, U.G., Werber, M.M., Beck, Y., Hartman, J.R., Frolow, F., & Sussman, J.L., 1989, J. Mol. Biol. 206, 787-788). Refinement of the protein structure (3,148 atoms with Mn and no solvents), with restraints maintaining noncrystallographic symmetry, converged at an R-factor of 0.207 using all data from 8.0 to 3.2 A resolution and group thermal parameters. The monomer-monomer interactions typical of bacterial Fe- and Mn-containing SODs are retained in the human enzyme, but the dimer-dimer interactions that form the tetramer are very different from those found in the structure of MnSOD from T. thermophilus. In human MnSOD one of the dimers is rotated by 84 degrees relative to its equivalent in the thermophile enzyme. As a result the monomers are arranged in an approximately tetrahedral array, the dimer-dimer packing is more intimate than observed in the bacterial MnSOD from T. thermophilus, and the dimers interdigitate. The metal-ligand interactions, determined by refinement and verified by computation of omit maps, are identical to those observed in T. thermophilus MnSOD.

About this StructureAbout this Structure

1MSD is a Single protein structure of sequence from Homo sapiens with as ligand. The following page contains interesting information on the relation of 1MSD with [Superoxide Dismutase]. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.

ReferenceReference

Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from Thermus thermophilus: differences in dimer-dimer interaction., Wagner UG, Pattridge KA, Ludwig ML, Stallings WC, Werber MM, Oefner C, Frolow F, Sussman JL, Protein Sci. 1993 May;2(5):814-25. PMID:8495200

Page seeded by OCA on Thu Feb 21 13:58:32 2008

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OCA

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-[[Image:1msd.gif|left|200px]]<br />
+[[Image:1msd.gif|left|200px]]<br /><applet load="1msd" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1msd" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1msd, resolution 3.2&Aring;" />
 '''COMPARISON OF THE CRYSTAL STRUCTURES OF GENETICALLY ENGINEERED HUMAN MANGANESE SUPEROXIDE DISMUTASE AND MANGANESE SUPEROXIDE DISMUTASE FROM THERMUS THERMOPHILUS. DIFFERENCES IN DIMER-DIMER INTERACTIONS.'''<br />
 ==Overview==
-The three-dimensional X-ray structure of a recombinant human mitochondrial, manganese superoxide dismutase (MnSOD) (chain length 198 residues) was, determined by the method of molecular replacement using the related, structure of MnSOD from Thermus thermophilus as a search model. This, tetrameric human MnSOD crystallizes in space group P2(1)2(1)2 with a dimer, in the asymmetric unit (Wagner, U.G., Werber, M.M., Beck, Y., Hartman, J.R., Frolow, F., &amp; Sussman, J.L., 1989, J. Mol. Biol. 206, 787-788)., Refinement of the protein structure (3,148 atoms with Mn and no solvents), with restraints maintaining noncrystallographic symmetry, converged at an, R-factor of 0.207 using all data from 8.0 to 3.2 A resolution and group, thermal parameters. The monomer-monomer interactions typical of bacterial, Fe- and Mn-containing SODs are retained in the human enzyme, but the, dimer-dimer interactions that form the tetramer are very different from, those found in the structure of MnSOD from T. thermophilus. In human MnSOD, one of the dimers is rotated by 84 degrees relative to its equivalent in, the thermophile enzyme. As a result the monomers are arranged in an, approximately tetrahedral array, the dimer-dimer packing is more intimate, than observed in the bacterial MnSOD from T. thermophilus, and the dimers, interdigitate. The metal-ligand interactions, determined by refinement and, verified by computation of omit maps, are identical to those observed in, T. thermophilus MnSOD.
+The three-dimensional X-ray structure of a recombinant human mitochondrial manganese superoxide dismutase (MnSOD) (chain length 198 residues) was determined by the method of molecular replacement using the related structure of MnSOD from Thermus thermophilus as a search model. This tetrameric human MnSOD crystallizes in space group P2(1)2(1)2 with a dimer in the asymmetric unit (Wagner, U.G., Werber, M.M., Beck, Y., Hartman, J.R., Frolow, F., &amp; Sussman, J.L., 1989, J. Mol. Biol. 206, 787-788). Refinement of the protein structure (3,148 atoms with Mn and no solvents), with restraints maintaining noncrystallographic symmetry, converged at an R-factor of 0.207 using all data from 8.0 to 3.2 A resolution and group thermal parameters. The monomer-monomer interactions typical of bacterial Fe- and Mn-containing SODs are retained in the human enzyme, but the dimer-dimer interactions that form the tetramer are very different from those found in the structure of MnSOD from T. thermophilus. In human MnSOD one of the dimers is rotated by 84 degrees relative to its equivalent in the thermophile enzyme. As a result the monomers are arranged in an approximately tetrahedral array, the dimer-dimer packing is more intimate than observed in the bacterial MnSOD from T. thermophilus, and the dimers interdigitate. The metal-ligand interactions, determined by refinement and verified by computation of omit maps, are identical to those observed in T. thermophilus MnSOD.
 ==About this Structure==
-MSD 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 MN as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1MSD with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb94_1.html Superoxide Dismutase]]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MSD OCA].
+MSD 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=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1MSD with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb94_1.html Superoxide Dismutase]]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MSD OCA].
 ==Reference==
@@ Line 16: / Line 15: @@
 [[Category: Superoxide Dismutase]]
 [[Category: Superoxide dismutase]]
-[[Category: Ludwig, M.L.]]
+[[Category: Ludwig, M L.]]
-[[Category: Pattridge, K.A.]]
+[[Category: Pattridge, K A.]]
 [[Category: Sussman, J.]]
-[[Category: Wagner, U.G.]]
+[[Category: Wagner, U G.]]
 [[Category: MN]]
 [[Category: oxidoreductase (superoxide acceptor)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:14:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:32 2008''