4hyd
From Proteopedia
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| - | [[ | + | ==Structure of a presenilin family intramembrane aspartate protease in C2221 space group== |
| + | <StructureSection load='4hyd' size='340' side='right' caption='[[4hyd]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4hyd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanoculleus_marisnigri_jr1 Methanoculleus marisnigri jr1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HYD FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hyc|4hyc]], [[4hyg|4hyg]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Memar_1924 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=368407 Methanoculleus marisnigri JR1])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hyd RCSB], [http://www.ebi.ac.uk/pdbsum/4hyd PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:23254940</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Methanoculleus marisnigri jr1]] | [[Category: Methanoculleus marisnigri jr1]] | ||
| - | [[Category: Dang, S | + | [[Category: Dang, S]] |
| - | [[Category: Li, X | + | [[Category: Li, X]] |
| - | [[Category: Shi, Y | + | [[Category: Shi, Y]] |
| - | [[Category: Wang, J | + | [[Category: Wang, J]] |
| - | [[Category: Yan, C | + | [[Category: Yan, C]] |
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Protease]] | [[Category: Protease]] | ||
Revision as of 16:45, 10 December 2014
Structure of a presenilin family intramembrane aspartate protease in C2221 space group
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