1ues
From Proteopedia
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| - | [[Image:1ues.gif|left|200px]] | + | [[Image:1ues.gif|left|200px]] |
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| - | '''Crystal structure of Porphyromonas gingivalis SOD''' | + | {{Structure |
| + | |PDB= 1ues |SIZE=350|CAPTION= <scene name='initialview01'>1ues</scene>, resolution 1.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Porphyromonas gingivalis SOD''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UES is a [ | + | 1UES is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UES OCA]. |
==Reference== | ==Reference== | ||
| - | Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site., Yamakura F, Sugio S, Hiraoka BY, Ohmori D, Yokota T, Biochemistry. 2003 Sep 16;42(36):10790-9. PMID:[http:// | + | Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site., Yamakura F, Sugio S, Hiraoka BY, Ohmori D, Yokota T, Biochemistry. 2003 Sep 16;42(36):10790-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12962504 12962504] |
[[Category: Porphyromonas gingivalis]] | [[Category: Porphyromonas gingivalis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: superoxide dismutase]] | [[Category: superoxide dismutase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:31:08 2008'' |
Revision as of 12:31, 20 March 2008
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| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Porphyromonas gingivalis SOD
Overview
Glycine 155, which is located approximately 10 A from the active metal sites, is mostly conserved in aligned amino acid sequences of manganese-specific superoxide dismutases (Mn-SODs) and cambialistic SOD (showing the same activity with Fe and Mn) from Porphyromonas gingivalis, but is substituted for threonine in most Fe-SODs. Since Thr155 is located between Trp123 and Trp125, and Trp123 is one member of the metal-surrounding aromatic amino acids, there is a possibility that the conversion of this amino acid may cause a conversion of the metal-specific activity of cambialistic P. gingivalis SOD. To clarify this possibility, we have prepared a mutant of the P. gingivalis SOD with conversion of Gly155 to Thr. The ratios of the specific activities of Fe- to Mn-reconstituted enzyme, which are measured by the xanthine oxidase/cytochrome c method, increased from 0.6 in the wild-type to 11.2 in the mutant SODs, indicating the conversion of the metal-specific activity of the enzyme from a cambialistic type to an Fe-specific type. The visible absorption spectra of the Fe- and Mn-reconstituted mutant SODs closely resembled those of Fe-specific SOD. Furthermore, the EPR spectra of the Fe- and Mn-reconstituted mutant SODs also closely resembled those of Fe-specific SOD. Three-dimensional structures of the Fe-reconstituted wild-type SOD and Mn-reconstituted mutant SOD have been determined at 1.6 A resolution. Both structures have identical conformations, orientations of residues involved in metal binding, and hydrogen bond networks, while the side chain of Trp123 is moved further toward the metal-binding site than in wild-type SOD. A possible contribution of the structural differences to the conversion of the metal-specific activity through rearrangement of the hydrogen bond network among Trp123, Gln70, Tyr35, and the metal-coordinated solvent is discussed.
About this Structure
1UES is a Single protein structure of sequence from Porphyromonas gingivalis. Full crystallographic information is available from OCA.
Reference
Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site., Yamakura F, Sugio S, Hiraoka BY, Ohmori D, Yokota T, Biochemistry. 2003 Sep 16;42(36):10790-9. PMID:12962504
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