1j3f
From Proteopedia
(New page: 200px<br /><applet load="1j3f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j3f, resolution 1.45Å" /> '''Crystal Structure of...) |
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| - | [[Image:1j3f.gif|left|200px]]<br /><applet load="1j3f" size=" | + | [[Image:1j3f.gif|left|200px]]<br /><applet load="1j3f" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1j3f, resolution 1.45Å" /> | caption="1j3f, resolution 1.45Å" /> | ||
'''Crystal Structure of an Artificial Metalloprotein:Cr(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin'''<br /> | '''Crystal Structure of an Artificial Metalloprotein:Cr(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | New methods for the synthesis of artificial metalloenzymes are important | + | New methods for the synthesis of artificial metalloenzymes are important for the construction of novel biocatalysts and biomaterials. Recently, we reported new methodology for the synthesis of artificial metalloenzymes by reconstituting apo-myoglobin with metal complexes (Ohashi, M. et al., Angew Chem., Int. Ed. 2003, 42, 1005-1008). However, it has been difficult to improve their reactivity, since their crystal structures were not available. In this article, we report the crystal structures of M(III)(Schiff base).apo-A71GMbs (M = Cr and Mn). The structures suggest that the position of the metal complex in apo-Mb is regulated by (i) noncovalent interaction between the ligand and surrounding peptides and (ii) the ligation of the metal ion to proximal histidine (His93). In addition, it is proposed that specific interactions of Ile107 with 3- and 3'-substituent groups on the salen ligand control the location of the Schiff base ligand in the active site. On the basis of these results, we have successfully controlled the enantioselectivity in the sulfoxidation of thioanisole by changing the size of substituents at the 3 and 3' positions. This is the first example of an enantioselective enzymatic reaction regulated by the design of metal complex in the protein active site. |
==About this Structure== | ==About this Structure== | ||
| - | 1J3F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with CR, PO4 and CZM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1J3F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=CR:'>CR</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=CZM:'>CZM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J3F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: schiff bases]] | [[Category: schiff bases]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:29 2008'' |
Revision as of 11:18, 21 February 2008
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Crystal Structure of an Artificial Metalloprotein:Cr(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin
Overview
New methods for the synthesis of artificial metalloenzymes are important for the construction of novel biocatalysts and biomaterials. Recently, we reported new methodology for the synthesis of artificial metalloenzymes by reconstituting apo-myoglobin with metal complexes (Ohashi, M. et al., Angew Chem., Int. Ed. 2003, 42, 1005-1008). However, it has been difficult to improve their reactivity, since their crystal structures were not available. In this article, we report the crystal structures of M(III)(Schiff base).apo-A71GMbs (M = Cr and Mn). The structures suggest that the position of the metal complex in apo-Mb is regulated by (i) noncovalent interaction between the ligand and surrounding peptides and (ii) the ligation of the metal ion to proximal histidine (His93). In addition, it is proposed that specific interactions of Ile107 with 3- and 3'-substituent groups on the salen ligand control the location of the Schiff base ligand in the active site. On the basis of these results, we have successfully controlled the enantioselectivity in the sulfoxidation of thioanisole by changing the size of substituents at the 3 and 3' positions. This is the first example of an enantioselective enzymatic reaction regulated by the design of metal complex in the protein active site.
About this Structure
1J3F is a Single protein structure of sequence from Physeter catodon with , and as ligands. Full crystallographic information is available from OCA.
Reference
Coordinated design of cofactor and active site structures in development of new protein catalysts., Ueno T, Koshiyama T, Ohashi M, Kondo K, Kono M, Suzuki A, Yamane T, Watanabe Y, J Am Chem Soc. 2005 May 11;127(18):6556-62. PMID:15869276
Page seeded by OCA on Thu Feb 21 13:18:29 2008
Categories: Physeter catodon | Single protein | Kono, M. | Koshiyama, T. | Ohashi, M. | Suzuki, A. | Ueno, T. | Watanabe, Y. | Yamane, T. | CR | CZM | PO4 | Asymmetric catalysis | Chromium | Crystal | Myoglobin | Schiff bases
