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논문 기본정보
Crystal Structure of Hypothetical Fructose-Specific EIIB from Escherichia coli
논문 개요
| 기관명 | NDSL |
|---|---|
| 저널명 | Molecules and cells |
| ISSN | 1016-8478,0219-1032 |
| ISBN |
논문저자 및 소속기관 정보
| 저자(한글) | Park, Jimin,Kim, Mi-Sun,Joo, Keehyung,Jhon, Gil-Ja,Berry, Edward A.,Lee, Jooyoung,Shin, Dong Hae |
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| 저자(영문) | |
| 소속기관 | |
| 소속기관(영문) | |
| 출판인 | |
| 간행물 번호 | |
| 발행연도 | 2016-01-01 |
| 초록 | We have solved the crystal structure of a predicted fructose-specific enzyme $IIB^{fruc}$ from Escherichia coli ( $EcEIIB^{fruc}$ ) involved in the phosphoenolpyruvate-carbohydrate phosphotransferase system transferring carbohydrates across the cytoplasmic membrane. $EcEIIB^{fruc}$ belongs to a sequence family with more than 5,000 sequence homologues with 25-99% amino-acid sequence identity. It reveals a conventional Rossmann-like ${ alpha}-{ beta}-{ alpha}$ sandwich fold with a unique ${ beta}$ -sheet topology. Its C-terminus is longer than its closest relatives and forms an additional ${ beta}$ -strand whereas the shorter C-terminus is random coil in the relatives. Interestingly, its core structure is similar to that of enzyme $IIB^{cellobiose}$ from E. coli ( $EcIIB^{cel}$ ) transferring a phosphate moiety. In the active site of the closest $EcEIIB^{fruc}$ homologues, a unique motif CXXGXAHT comprising a P-loop like architecture including a histidine residue is found. The conserved cysteine on this loop may be deprotonated to act as a nucleophile similar to that of $EcIIB^{cel}$ . The conserved histidine residue is presumed to bind the negatively charged phosphate. Therefore, we propose that the catalytic mechanism of $EcEIIB^{fruc}$ is similar to that of $EcIIB^{cel}$ transferring phosphoryl moiety to a specific carbohydrate. |
| 원문URL | http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=03553784&target=NART&cn=JAKO201621650492519 |
| 첨부파일 |
추가정보
| 과학기술표준분류 | |
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| ICT 기술분류 | |
| DDC 분류 | |
| 주제어 (키워드) | frwD,fructose specific enzyme EIIB,functional cysteine,PTS permease,PTS system,X-ray crystallography |