5X3F

Crystal structure of the YgjG-Protein A-Zpa963-PKA catalytic domain

5X3F の概要

• エントリーDOI: 10.2210/pdb5x3f/pdb
• 分子名称: Putrescine aminotransferase,Immunoglobulin G-binding protein A, Zpa963,cAMP-dependent protein kinase catalytic subunit alpha (2 entities in total)
• 機能のキーワード: synthetic protein, lyase, transferase
• 由来する生物種: Escherichia coli (strain K12); 詳細
• 細胞内の位置: Secreted, cell wall ; Peptidoglycan-anchor : P38507; Cytoplasm . Isoform 2: Cell projection, cilium, flagellum : P05132
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99931.20

構造登録者

Youn, S.J.,Kwon, N.Y.,Lee, J.H.,Kim, J.H.,Lee, H.,Lee, J.O. (登録日: 2017-02-05, 公開日: 2017-06-28, 最終更新日: 2023-11-22)

主引用文献

Youn, S.J.,Kwon, N.Y.,Lee, J.H.,Kim, J.H.,Choi, J.,Lee, H.,Lee, J.O.
Construction of novel repeat proteins with rigid and predictable structures using a shared helix method.
Sci Rep, 7:2595-2595, 2017

PubMed Abstract: Generating artificial protein assemblies with complex shapes requires a method for connecting protein components with stable and predictable structures. Currently available methods for creating rigid protein assemblies rely on either complicated calculations or extensive trial and error. We describe a simple and efficient method for connecting two proteins via a fused alpha helix that is formed by joining two preexisting helices into a single extended helix. Because the end-to-end ligation of helices does not guarantee the formation of a continuous helix, we superimposed 1-2 turns of pairs of connecting helices by using a molecular graphics program. Then, we chose amino acids from the two natural sequences that would stabilize the connecting helix. This "shared helix method" is highly efficient. All the designed proteins that could be produced in Escherichia coli were readily crystallized and had the expected fusion structures. To prove the usefulness of this method, we produced two novel repeat proteins by assembling several copies of natural or artificial proteins with alpha helices at both termini. Their crystal structures demonstrated the successful assembly of the repeating units with the intended curved shapes. We propose that this method could dramatically expand the available repertoire of natural repeat proteins.

PubMed: 28572639
DOI: 10.1038/s41598-017-02803-z

実験手法

X-RAY DIFFRACTION (3.38 Å)