2V9M

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A87M- T109F-E192A)

2V9M の概要

• エントリーDOI: 10.2210/pdb2v9m/pdb
• 関連するPDBエントリー: 1GT7 1OJR 2UYU 2UYV 2V29 2V2A 2V2B 2V9E 2V9F 2V9G 2V9I 2V9L 2V9N 2V9O
• 分子名称: RHAMNULOSE-1-PHOSPHATE ALDOLASE, ZINC ION, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: entropy index, metal-binding, oligomerization, zinc, lyase, aldolase, class ii, cytoplasm, cleavage of l-rhamnulose-1-phosphate to dihydroxyacetoneph bacterial l-rhamnose metabolism, interface design, surface mutation, 2-ketose degradation, protein-protein interface, rare sugar, aggregation, zinc enzyme, fibrillation, rhamnose metabolism, protein engineering
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61435.50

構造登録者

Grueninger, D.,Schulz, G.E. (登録日: 2007-08-24, 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 (1.3 Å)