1YZC

The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N- and a part of the C-terminal helices unfolded

Summary for 1YZC

• Entry DOI: 10.2210/pdb1yzc/pdb
• Related: 1YZA
• NMR Information: BMRB: 6552
• Descriptor: edesigned apo-cytochrome b562 (1 entity in total)
• Functional Keywords: folding intermediates, native-state hydrogen exchange, protein engineering, protein structure, structural genomics, psi, protein structure initiative, berkeley structural genomics center, bsgc, electron transport
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 11179.26

Authors

Feng, H.,Zhou, Z.,Bai, Y.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2005-02-28, release date: 2006-03-28, Last modification date: 2024-05-29)

Primary citation

Feng, H.,Zhou, Z.,Bai, Y.
A protein folding pathway with multiple folding intermediates at atomic resolution
Proc.Natl.Acad.Sci.Usa, 102:5026-5031, 2005

PubMed Abstract: Using native-state hydrogen-exchange-directed protein engineering and multidimensional NMR, we determined the high-resolution structure (rms deviation, 1.1 angstroms) for an intermediate of the four-helix bundle protein: Rd-apocytochrome b562. The intermediate has the N-terminal helix and a part of the C-terminal helix unfolded. In earlier studies, we also solved the structures of two other folding intermediates for the same protein: one with the N-terminal helix alone unfolded and the other with a reorganized hydrophobic core. Together, these structures provide a description of a protein folding pathway with multiple intermediates at atomic resolution. The two general features for the intermediates are (i) native-like backbone topology and (ii) nonnative side-chain interactions. These results have implications for important issues in protein folding studies, including large-scale conformation search, -value analysis, and computer simulations.

PubMed: 15793003
DOI: 10.1073/pnas.0501372102

Experimental method

SOLUTION NMR