1ufp: Difference between revisions
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'''Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-wild type Myoglobin''' | '''Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-wild type Myoglobin''' | ||
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[[Category: Watanabe, Y.]] | [[Category: Watanabe, Y.]] | ||
[[Category: Yamane, T.]] | [[Category: Yamane, T.]] | ||
[[Category: | [[Category: Iron]] | ||
[[Category: | [[Category: Metalloprotein]] | ||
[[Category: | [[Category: Myoglobin]] | ||
[[Category: | [[Category: Salophen]] | ||
[[Category: | [[Category: Schiff base]] | ||
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Revision as of 08:09, 3 May 2008
Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-wild type Myoglobin
Overview
Apo-myoglobin (apo-Mb) and apo-A71GMb were successfully reconstituted with FeIII(salophen) (1) (salophen = N,N'-bis(salicylidene)-1,2-phenilenediamine), Fe(III)(3,3'-Me2-salophen) (2), and FeIII(5,5'-t-Bu2-salophen) (3). The crystal structure of 2.apo-A71GMb shows the tight binding of the complex in the Mb cavity, while in wild-type apo-Mb it is highly disordered due to the steric repulsion with Ala71. Furthermore, the structure of 2.apo-A71GMb suggests a possible accommodation of a small substrate in the cavity. In fact, the cyanide association rate constant of 2.apo-A71GMb is 216-fold larger compared to that of 2.apo-Mb. These results provide us principles for the noncovalent fixation of synthetic metal cofactors at the desired positions in protein matrixes.
About this Structure
1UFP is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
Reference
Crystal structures of artificial metalloproteins: tight binding of FeIII(Schiff-Base) by mutation of Ala71 to Gly in apo-myoglobin., Ueno T, Ohashi M, Kono M, Kondo K, Suzuki A, Yamane T, Watanabe Y, Inorg Chem. 2004 May 3;43(9):2852-8. PMID:15106972 Page seeded by OCA on Sat May 3 11:09:32 2008
