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Solution structure of apocytochrome b562.

Feng Y, Sligar SG, Wand AJ
Nat Struct Biol 1 30-5 (1994)
Cited: 61 times
EuropePMC logo PMID: 7656004

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.

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Related citations provided by authors (1)

  1. 1H and 15N NMR Resonance Assignments and Preliminary Structural Characterization of Escherichia Coli Apocytochrome B562. Feng Y, Wand AJ, Sligar SG Biochemistry 30 7711- (1991)

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