Structural highlights
Function
[C562_ECOLX] Electron-transport protein of unknown function.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure of apocytochrome b562.,Feng Y, Sligar SG, Wand AJ Nat Struct Biol. 1994 Jan;1(1):30-5. PMID:7656004[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Feng Y, Sligar SG, Wand AJ. Solution structure of apocytochrome b562. Nat Struct Biol. 1994 Jan;1(1):30-5. PMID:7656004
