1MFT

Crystal Structure Of Four-Helix Bundle Model

Summary for 1MFT

• Entry DOI: 10.2210/pdb1mft/pdb
• Related: 1EC5 1JMB 1JMO
• Descriptor: Four-helix bundle model, ZINC ION (3 entities in total)
• Functional Keywords: alpha-helical bundle, protein design, helix turn helix, de novo protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 13085.61

Authors

Lahr, S.J.,Stayrook, S.E.,North, B.,Kaplan, J.,Geremia, S.,DeGrado, W. (deposition date: 2002-08-13, release date: 2004-01-20, Last modification date: 2024-02-14)

Primary citation

Lahr, S.J.,Engel, D.E.,Stayrook, S.E.,Maglio, O.,North, B.,Geremia, S.,Lombardi, A.,DeGrado, W.F.
Analysis and Design of Turns in alpha-Helical Hairpins
J.Mol.Biol., 346:1441-1454, 2005

PubMed Abstract: Although the analysis and design of turns that connect the strands in antiparallel beta-hairpins has reached an advanced state, much less is known concerning turns between antiparallel helices in helical hairpins. We have conducted an analysis of the structures and sequence preferences of two types of interhelical turns, each of which connects the two helices by a two-residue linker in an alphaL-beta conformation. Based on this analysis, it became apparent that the turn introduced into a designed four-helix bundle protein, DF1, did not occur within an optimal structural context. DF1 is a dimeric model for the diiron class of proteins. A longer loop with a beta-alphaR-beta conformation was inserted between two helices in the protein, and a sequence was chosen to stabilize its conformation. X-ray crystallography and NMR analysis of the protein showed the structure to be in excellent agreement with design.

PubMed: 15713492
DOI: 10.1016/j.jmb.2004.12.016

Experimental method

X-RAY DIFFRACTION (2.5 Å)