2V7G

Crystal Structure of an Engineered Urocanase Tetramer

2V7G の概要

• エントリーDOI: 10.2210/pdb2v7g/pdb
• 関連するPDBエントリー: 1UWK 1UWL 1W1U
• 分子名称: UROCANATE HYDRATASE, ACETATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: histidine degradation, nad, lyase, protein engineering, urocanate hydratase, histidine metabolism
• 由来する生物種: PSEUDOMONAS PUTIDA
• 細胞内の位置: Cytoplasm: P25080
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 247142.59

構造登録者

Treiber, N.,Schulz, G.E. (登録日: 2007-07-30, 公開日: 2008-01-15, 最終更新日: 2023-12-13)

主引用文献

Grueninger, D.,Treiber, N.,Ziegler, M.O.P.,Koetter, J.W.A.,Schulze, M.-S.,Schulz, G.E.
Designed Protein-Protein Association.
Science, 319:206-, 2008

PubMed Abstract: The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface. Symmetry plays an important role because it defines the multiplicity of a designed contact and therefore the number of required mutations. Some of the proteins needed only a single side-chain alteration in order to associate to a higher-order complex. The mobility of the buried side chains has to be taken into account. Four assemblies have been structurally elucidated. Comparisons between the designed contacts and the results will provide useful guidelines for the development of future architectures.

PubMed: 18187656
DOI: 10.1126/SCIENCE.1150421

実験手法

X-RAY DIFFRACTION (2 Å)