1APC

SOLUTION STRUCTURE OF APOCYTOCHROME B562

Summary for 1APC

• Entry DOI: 10.2210/pdb1apc/pdb
• Descriptor: CYTOCHROME B562 (1 entity in total)
• Functional Keywords: electron transport
• Biological source: Escherichia coli
• Cellular location: Periplasm : P0ABE7
• Total number of polymer chains: 1
• Total formula weight: 11799.24

Authors

Wand, A.J.,Feng, Y.,Sligar, S.G. (deposition date: 1993-10-14, release date: 1994-01-31, Last modification date: 2024-04-10)

Primary citation

Feng, Y.,Sligar, S.G.,Wand, A.J.
Solution structure of apocytochrome b562.
Nat.Struct.Biol., 1:30-35, 1994

PubMed 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.

PubMed: 7656004
DOI: 10.1038/nsb0194-30

Experimental method

SOLUTION NMR