| 학회 |
한국화학공학회 |
| 학술대회 |
2017년 가을 (10/25 ~ 10/27, 대전컨벤션센터) |
| 권호 |
23권 2호, p.1744 |
| 발표분야 |
생물화공 |
| 제목 |
X-ray Crystal Structure of PAT Protein-Aptamer Complex |
| 초록 |
Phosphinothricin N-acetyltransferase (PAT) is a herbicide-resistant protein that is inactivate to the glufosinate in genetically modified organism (GMO). Detection system for GM crops are important for its regulation. Aptamer is single-stranded DNA or RNA oligonucleotides that can bind to target molecule with high affinity and selectivity. Structural analysis of protein-aptamer complexes can helps in understanding its functions and interactions. In this study, we set up PAT crystallization for structural analysis of PAT with and without aptamer. The PAT gene was cloned in pET-21a and expressed by E.coli BL21 (DE3). The protein was purified by three step purification: Affinity chromatography, Ion-exchange chromatography and Gel filtration chromatography. Sitting drop vapor diffusion was used for crystallization at 291K temperature. By analyzing the structure of PAT protein-aptamer complex, it can be used to identify important functions. This work was carried out with the support of "Cooperative Research Program for Agriculture Science & Technology Development (Project No. PJ012568)" Rural Development Administration, Republic of Korea. |
| 저자 |
이진표1, 신우리1, Simranjeet Singh Sekhon1, 안지영1, 민지호2, 김양훈1
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| 소속 |
1충북대, 2전북대 |
| 키워드 |
생물화공 |
| E-Mail |
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| 원문파일 |
초록 보기 |
