1nz5: Difference between revisions

Revision as of 13:33, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nz5.png

Template:STRUCTURE 1nz5

The Horse heart myoglobin variant K45E/K63E complexed with ManganeseThe Horse heart myoglobin variant K45E/K63E complexed with Manganese

Template:ABSTRACT PUBMED 12644706

About this StructureAbout this Structure

1NZ5 is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

ReferenceReference

Introduction and characterization of a functionally linked metal ion binding site at the exposed heme edge of myoglobin., Hunter CL, Maurus R, Mauk MR, Lee H, Raven EL, Tong H, Nguyen N, Smith M, Brayer GD, Mauk AG, Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3647-52. Epub 2003 Mar 18. PMID:12644706

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The Horse heart myoglobin variant K45E/K63E complexed with Manganese'''
+===The Horse heart myoglobin variant K45E/K63E complexed with Manganese===
-==Overview==
+<!--
-A binding site for metal ions has been created on the surface of horse heart myoglobin (Mb) near the heme 6-propionate group by replacing K45 and K63 with glutamyl residues. One-dimensional (1)H NMR spectroscopy indicates that Mn(2+) binds in the vicinity of the heme 6-propionate as anticipated, and potentiometric titrations establish that the affinity of the new site for Mn(2+) is 1.28(4) x 10(4) M(-1) (pH 6.96, ionic strength I = 17.2 microM, 25 degrees C). In addition, these substitutions lower the reduction potential of the protein and increase the pK(a) for the water molecule coordinated to the heme iron of metmyoglobin. The peroxidase [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid), ABTS, as substrate] and the Mn(2+)-peroxidase activity of the variant are both increased approximately 3-fold. In contrast to wild-type Mb, both the affinity for azide and the midpoint potential of the variant are significantly influenced by the addition of Mn(2+). The structure of the variant has been determined by x-ray crystallography to define the coordination environment of bound Mn(2+) and Cd(2+). Although slight differences are observed between the geometry of the binding of the two metal ions, both are hexacoordinate, and neither involves coordination by E63.
+The line below this paragraph, {{ABSTRACT_PUBMED_12644706}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12644706}}
 ==About this Structure==
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 [[Category: Tong, H.]]
 [[Category: Manganese mn2+ horse heart myoglobin engineered metal binding site]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:09:48 2008''
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