3O2E

Crystal structure of a bol-like protein from babesia bovis

3O2E の概要

• エントリーDOI: 10.2210/pdb3o2e/pdb
• 関連するPDBエントリー: 3K9G 3KM3 3KW3 3LUZ 3MEN 3NJB 3OIB 3P96 3PFD 3PM6
• 分子名称: BolA-like protein, IODIDE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: ssgcid, babesia bovis, iodide, sad, seattle structural genomics center for infectious disease, bol like protein, unknown function
• 由来する生物種: Babesia bovis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12767.68

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2010-07-22, 公開日: 2010-10-13, 最終更新日: 2024-11-06)

主引用文献

Abendroth, J.,Gardberg, A.S.,Robinson, J.I.,Christensen, J.S.,Staker, B.L.,Myler, P.J.,Stewart, L.J.,Edwards, T.E.
SAD phasing using iodide ions in a high-throughput structural genomics environment.
J.Struct.Funct.Genom., 12:83-95, 2011

PubMed Abstract: The Seattle Structural Genomics Center for Infectious Disease (SSGCID) focuses on the structure elucidation of potential drug targets from class A, B, and C infectious disease organisms. Many SSGCID targets are selected because they have homologs in other organisms that are validated drug targets with known structures. Thus, many SSGCID targets are expected to be solved by molecular replacement (MR), and reflective of this, all proteins are expressed in native form. However, many community request targets do not have homologs with known structures and not all internally selected targets readily solve by MR, necessitating experimental phase determination. We have adopted the use of iodide ion soaks and single wavelength anomalous dispersion (SAD) experiments as our primary method for de novo phasing. This method uses existing native crystals and in house data collection, resulting in rapid, low cost structure determination. Iodide ions are non-toxic and soluble at molar concentrations, facilitating binding at numerous hydrophobic or positively charged sites. We have used this technique across a wide range of crystallization conditions with successful structure determination in 16 of 17 cases within the first year of use (94% success rate). Here we present a general overview of this method as well as several examples including SAD phasing of proteins with novel folds and the combined use of SAD and MR for targets with weak MR solutions. These cases highlight the straightforward and powerful method of iodide ion SAD phasing in a high-throughput structural genomics environment.

PubMed: 21359836
DOI: 10.1007/s10969-011-9101-7

実験手法

X-RAY DIFFRACTION (1.95 Å)