NDLI: Miniaturized metalloproteins: Application to iron

Content Provider	PubMed Central
Author	Lombardi, Angela Marasco, Daniela Maglio, Ornella Costanzo, Luigi Di Nastri, Flavia Pavone, Vincenzo
Copyright Year	2000
Abstract	The miniaturization process applied to rubredoxins generated a class of peptide-based metalloprotein models, named METP (miniaturized electron transfer protein). The crystal structure of Desulfovibrio vulgaris rubredoxin was selected as a template for the construction of a tetrahedral (Sγ-Cys)4 iron-binding site. Analysis of the structure showed that a sphere of 17 Å in diameter, centered on the metal, circumscribes two unconnected approximately C2 symmetry related β-hairpins, each containing the -Cys-(Aaa)2-Cys- sequence. These observations provided a starting point for the design of an undecapeptide, which self assembles in the presence of tetrahedrally coordinating metal ions. The METP peptide was synthesized in good yield by standard methodologies. Successful assembly of the METP peptide with Co(II), Zn(II), Fe(II/III), in the expected 2:1 stoichiometry, was proven by UV-visible and circular dichroism spectroscopies. UV-visible analysis of the metal complexes indicated the four Cys ligands tetrahedrally arrange around the metal ion, as designed. Circular dichroism measurements on both the free and metal-bound forms revealed that the metal coordination drives the peptide chain to fold into a turned conformation. NMR characterization of the Zn(II)-METP complex fully supported the structure of the designed model. These results prove that METP reproduces the main features of rubredoxin.
Related Links	http://dx.doi.org/10.1073/pnas.97.22.11922
Ending Page	11927
Page Count	6
Starting Page	11922
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	22
Volume Number	97
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2000-10-24
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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