1AE2

MUTANT L32R OF GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)

1AE2 の概要

• エントリーDOI: 10.2210/pdb1ae2/pdb
• 分子名称: GENE V PROTEIN (2 entities in total)
• 機能のキーワード: single-stranded dna binding protein, gvp, l32r, mutant, dna-binding protein, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9743.25

構造登録者

Su, S.,Gao, Y.-G.,Zhang, H.,Terwilliger, T.C.,Wang, A.H.-J. (登録日: 1997-03-04, 公開日: 1997-09-04, 最終更新日: 2024-02-07)

主引用文献

Su, S.,Gao, Y.G.,Zhang, H.,Terwilliger, T.C.,Wang, A.H.
Analyses of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography.
Protein Sci., 6:771-780, 1997

PubMed Abstract: The high-resolution crystal structure of the gene V protein (GVP) from the Ff filamentous phages (M13, fl, fd) has been solved recently for the wild-type and two surface mutant (Y41F and Y41H) proteins, leading to a plausible model for the polymeric GVP-ssDNA complex (Guan Y, Zhang H, Wang AHJ, 1995, Protein Sci 4:187-197). The model of the complex shows extensive contacts between neighboring dimer GVPs involving electrostatic interactions between the K69 from one and the D79 and R82 from the next dimer. In addition, hydrophobic interactions between the amino acids L32 and L44 from one and G23 from the next dimer also contribute to the dimer-dimer interactions. Mutations at the L32, K69, and R82 amino acid sites generally destabilize the protein and many of these affect the function of the phage. We have studied the structural effects of three mutant proteins involving those sites, i.e., L32R, K69H, and R82C, by X-ray crystallographic analysis at 2.0 A resolution. In L32R GVP, the structural perturbation is localized, whereas in K69H and R82C GVPs, some long-range effects are also detected in addition to the local perturbation. We have interpreted the protein stability and the functional properties associated with those mutations in terms of the observed structural perturbations.

PubMed: 9098886

実験手法

X-RAY DIFFRACTION (2 Å)