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1uer
From Proteopedia
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[[Image:1uer.gif|left|200px]] | [[Image:1uer.gif|left|200px]] | ||
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'''Crystal structure of Porphyromonas gingivalis SOD''' | '''Crystal structure of Porphyromonas gingivalis SOD''' | ||
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[[Category: Yamakura, F.]] | [[Category: Yamakura, F.]] | ||
[[Category: Yokota, T.]] | [[Category: Yokota, T.]] | ||
| - | [[Category: | + | [[Category: Cambialistic]] |
| - | [[Category: | + | [[Category: Metal-specific]] |
| - | [[Category: | + | [[Category: Sod]] |
| - | [[Category: | + | [[Category: Superoxide dismutase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:07:16 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:07, 3 May 2008
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
1UER 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 Page seeded by OCA on Sat May 3 11:07:16 2008
