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New page: left|200px<br /><applet load="1uer" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uer, resolution 1.6Å" /> '''Crystal structure of ...
 
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[[Image:1uer.gif|left|200px]]<br /><applet load="1uer" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1uer.gif|left|200px]]<br /><applet load="1uer" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1uer, resolution 1.6&Aring;" />
caption="1uer, resolution 1.6&Aring;" />
'''Crystal structure of Porphyromonas gingivalis SOD'''<br />
'''Crystal structure of Porphyromonas gingivalis SOD'''<br />


==Overview==
==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.
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==
==About this Structure==
1UER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1UER OCA].  
1UER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1UER OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Superoxide dismutase]]
[[Category: Superoxide dismutase]]
[[Category: Hiraoka, B.Y.]]
[[Category: Hiraoka, B Y.]]
[[Category: Ohmori, D.]]
[[Category: Ohmori, D.]]
[[Category: Sugio, S.]]
[[Category: Sugio, S.]]
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[[Category: superoxide dismutase]]
[[Category: superoxide dismutase]]


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