Solution structure of apocytochrome b562. Academic Article

abstract

• The apoprotein is an important intermediate on the folding pathways of many haem proteins, yet a detailed structure of such an intermediate has remained elusive. Here we present the structure of apocytochrome b562 obtained by NMR spectroscopy. The apoprotein has a topology similar to the holoprotein. Nevertheless, significant differences in helix-helix packing between the two are evident. Much of the haem binding pocket in the apoprotein is preserved but exposed to solvent creating a large cavern. As apocytochrome b562 displays many of the physical characteristics ascribed to the molten globule state, these results help ellucidate the origin of several properties of the protein molten globule.

authors

• Wand, Joshua

published proceedings

• Nat Struct Biol

author list (cited authors)

• Feng, Y., Sligar, S. G., & Wand, A. J.

citation count

• 124

complete list of authors

• Feng, Y||Sligar, SG||Wand, AJ

publication date

• January 1994

publisher

• Springer Nature  Publisher

published in

• Nature Structural and Molecular Biology  Journal

keywords

• Apoproteins
• Binding Sites
• Cytochrome B Group
• Escherichia Coli
• Heme
• Magnetic Resonance Spectroscopy
• Models, Molecular
• Molecular Structure
• Protein Conformation
• Protein Folding
• Protein Structure, Tertiary
• Solutions

PubMed Central ID

• 7656004

Digital Object Identifier (DOI)

• 10.1038/nsb0194-30

start page

• 30

end page

• 35

volume

• 1

issue

• 1

URL

• http://dx.doi.org/10.1038/nsb0194-30