1ufp

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spinqualitylabelsall models 1ufp, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 with PO4 as ligand. 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

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