4hyc | pdb_00004hyc

Structure of a presenilin family intramembrane aspartate protease in P2 space group

spinqualitylabelsall models 4hyc, resolution 3.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hyc is a 8 chain structure with sequence from Methanoculleus marisnigri JR1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A3CWV0_METMJ Publication Abstract from PubMed Presenilin and signal peptide peptidase (SPP) are intramembrane aspartyl proteases that regulate important biological functions in eukaryotes. Mechanistic understanding of presenilin and SPP has been hampered by lack of relevant structural information. Here we report the crystal structure of a presenilin/SPP homologue (PSH) from the archaeon Methanoculleus marisnigri JR1. The protease, comprising nine transmembrane segments (TMs), adopts a previously unreported protein fold. The amino-terminal domain, consisting of TM1-6, forms a horseshoe-shaped structure, surrounding TM7-9 of the carboxy-terminal domain. The two catalytic aspartate residues are located on the cytoplasmic side of TM6 and TM7, spatially close to each other and approximately 8 A into the lipid membrane surface. Water molecules gain constant access to the catalytic aspartates through a large cavity between the amino- and carboxy-terminal domains. Structural analysis reveals insights into the presenilin/SPP family of intramembrane proteases. Structure of a presenilin family intramembrane aspartate protease.,Li X, Dang S, Yan C, Gong X, Wang J, Shi Y Nature. 2012 Dec 19. doi: 10.1038/nature11801. PMID:23254940 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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