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Atg3 has an/-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region, one of which consists of80 residues and has a random coil structure in solution and another with a long -helical structure that protrudes from the core region as far as 30A˚ . In vivo and in vitro analyses suggested that the former region is responsible for binding Atg7, an E1-like enzyme, and that the latter is responsible for binding Atg8.Asulfate ion was bound near the catalytic cysteine of Atg3, suggesting a possible binding site for the phosphate moiety of PE. |
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3Â¥2014-11-19 11:10:36
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- ·ÒëEPI: 1690
- Ó¦Öú: 452 (˶ʿ)
- ½ð±Ò: 31580.9
- ºì»¨: 100
- Ìû×Ó: 7681
- ÔÚÏß: 19966.6Сʱ
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°®ÓëÓêÏÂ: ½ð±Ò+1 2014-11-19 06:39:39
¹Ô±¦ÎÄÎÄ: ½ð±Ò+30, ·ÒëEPI+1 2014-11-19 11:16:06
°®ÓëÓêÏÂ: ½ð±Ò+1 2014-11-19 06:39:39
¹Ô±¦ÎÄÎÄ: ½ð±Ò+30, ·ÒëEPI+1 2014-11-19 11:16:06
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