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[资源] 《自然》【nature】2013年1月3日全文PDF版本

清华大学施一公教授的文章
Structure of a presenilin family intramembrane aspartate protease
Xiaochun Li1,2*, Shangyu Dang1,2*, Chuangye Yan1,2, Xinqi Gong1,2, JiaweiWang2,3 & Yigong Shi1,2
Presenilin and signal peptide peptidase (SPP) are intramembrane aspartyl proteases that regulate important biologicalfunctions in eukaryotes.Mechanisticunderstandingof presenilin and SPPhas been hamperedby relevantstructuralinformation.Herewereport the crystal structure of a presenilin/SPPhomologue (PSH) fromthearchaeonMethanoculleusmarisnigri JR1. The protease, comprising nine transmembrane segments (TMs), adopts a previously unreported protein. The amino-terminal domain, consisting of TM1–6, forms a horseshoe-shaped structure, surrounding TM7–9 of thecarboxy-terminal domain. The two catalytic aspartate residues are located on the cytoplasmic side of TM6 and TM7,spatially close to each other and approximately 8A˚ into the lipid membrane surface. Water molecules gain constantaccess to the catalytic aspartates through a large cavity between the amino- and carboxy-terminal domains. Structuralanalysis reveals insights into the presenilin/SPP family of intramembrane proteases.
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附件 1 : Nature2013-1-3.pdf

2013-01-04 19:34:43, 32.71 M

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