2GBM

Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin

2GBM の概要

• エントリーDOI: 10.2210/pdb2gbm/pdb
• 関連するPDBエントリー: 2GBJ 2GBK 2GBN 2GBR
• 分子名称: Ubiquitin, ARSENIC (3 entities in total)
• 機能のキーワード: loop insertion, protein binding
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 36357.74

構造登録者

Ferraro, D.M.,Ferraro, D.J.,Ramaswamy, S.,Robertson, A.D. (登録日: 2006-03-10, 公開日: 2006-05-16, 最終更新日: 2023-08-30)

主引用文献

Ferraro, D.M.,Ferraro, D.J.,Ramaswamy, S.,Robertson, A.D.
Structures of Ubiquitin Insertion Mutants Support Site-specific Reflex Response to Insertions Hypothesis.
J.Mol.Biol., 359:390-402, 2006

PubMed Abstract: We previously concluded that, judging from NMR chemical shifts, the effects of insertions into ubiquitin on its conformation appear to depend primarily on the site of insertion rather than the sequence of the insertion. To obtain a more complete and atomic-resolution understanding of how these insertions modulate the conformation of ubiquitin, we have solved the crystal structures of four insertional mutants of ubiquitin. Insertions between residues 9 and 10 of ubiquitin are minimally perturbing to the remainder of the protein, while larger alterations occur when the insertion is between residues 35 and 36. Further, the alterations in response to insertions are very similar for each mutant at a given site. Two insertions, one at each site, were designed from structurally homologous proteins. Interestingly, the secondary structure within these five to seven amino acid residue insertions is conserved in the new protein. Overall, the crystal structures support the previous conclusion that the conformational effects of these insertions are determined largely by the site of insertion and only secondarily by the sequence of the insert.

PubMed: 16647719
DOI: 10.1016/j.jmb.2006.03.047

実験手法

X-RAY DIFFRACTION (1.55 Å)