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1uer

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[[Image:1uer.gif|left|200px]]
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{{STRUCTURE_1uer| PDB=1uer | SCENE= }}
{{STRUCTURE_1uer| PDB=1uer | SCENE= }}
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'''Crystal structure of Porphyromonas gingivalis SOD'''
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===Crystal structure of Porphyromonas gingivalis SOD===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12962504 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12962504}}
==About this Structure==
==About this Structure==
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==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://www.ncbi.nlm.nih.gov/pubmed/12962504 12962504]
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]
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Crystal structure of cambialistic superoxide dismutase from porphyromonas gingivalis., Sugio S, Hiraoka BY, Yamakura F, Eur J Biochem. 2000 Jun;267(12):3487-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10848964 10848964]
[[Category: Porphyromonas gingivalis]]
[[Category: Porphyromonas gingivalis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Sod]]
[[Category: Sod]]
[[Category: Superoxide dismutase]]
[[Category: Superoxide dismutase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:07:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:31:04 2008''

Revision as of 17:31, 27 July 2008

Image:1uer.png

Template:STRUCTURE 1uer

Crystal structure of Porphyromonas gingivalis SOD

Template:ABSTRACT PUBMED 12962504

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

Crystal structure of cambialistic superoxide dismutase from porphyromonas gingivalis., Sugio S, Hiraoka BY, Yamakura F, Eur J Biochem. 2000 Jun;267(12):3487-95. PMID:10848964

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