1T8K

Crystal Structure of apo acyl carrier protein from E. coli

1T8K の概要

• エントリーDOI: 10.2210/pdb1t8k/pdb
• 分子名称: Acyl carrier protein, ZINC ION, IMIDAZOLE, ... (4 entities in total)
• 機能のキーワード: acp, lipid transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A6A8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9582.86

構造登録者

Qiu, X.,Janson, C.A. (登録日: 2004-05-13, 公開日: 2004-09-07, 最終更新日: 2024-02-14)

主引用文献

Qiu, X.,Janson, C.A.
Structure of apo acyl carrier protein and a proposal to engineer protein crystallization through metal ions.
Acta Crystallogr.,Sect.D, 60:1545-1554, 2004

PubMed Abstract: A topic of current interest is engineering surface mutations in order to improve the success rate of protein crystallization. This report explores the possibility of using metal-ion-mediated crystal-packing interactions to facilitate rational design. Escherichia coli apo acyl carrier protein was chosen as a test case because of its high content of negatively charged carboxylates suitable for metal binding with moderate affinity. The protein was successfully crystallized in the presence of zinc ions. The crystal structure was determined to 1.1 A resolution with MAD phasing using anomalous signals from the co-crystallized Zn(2+) ions. The case study suggested an integrated strategy for crystallization and structure solution of proteins via engineering surface Asp and Glu mutants, crystallizing them in the presence of metal ions such as Zn(2+) and solving the structures using anomalous signals.

PubMed: 15333924
DOI: 10.1107/S0907444904015422

実験手法

X-RAY DIFFRACTION (1.1 Å)