This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4kwb
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Structure of signal peptide peptidase A with C-termini bound in the active sites: insights into specificity, self-processing and regulation== | |
| - | + | <StructureSection load='4kwb' size='340' side='right' caption='[[4kwb]], [[Resolution|resolution]] 2.39Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4kwb]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KWB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KWB FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bez|3bez]], [[3bfo|3bfo]], [[3rst|3rst]]</td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU29530, CLONED SIGNAL PEPTIDE PEPTIDASE A GENE FROM RESIDUES 26 TO 335, LYS199 MUTATED TO ALA, sppA, yteI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=4kwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kwb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kwb RCSB], [http://www.ebi.ac.uk/pdbsum/4kwb PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/SPPA_BACSU SPPA_BACSU]] Digestion of cleaved signal peptides (By similarity). Required for efficient processing of precursors under conditions of hyper-secretion. | [[http://www.uniprot.org/uniprot/SPPA_BACSU SPPA_BACSU]] Digestion of cleaved signal peptides (By similarity). Required for efficient processing of precursors under conditions of hyper-secretion. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacterial signal peptide peptidase A (SppA) is a membrane-bound enzyme that utilizes a serine/lysine catalytic dyad mechanism to cleave remnant signal peptides within the cellular membrane. Bacillus subtilis SppA (SppABS) oligomerizes into a homo-octameric dome-shaped complex with eight active sites, located at the interface between each protomer. In this study, we show that SppABS self-processes its own C-termini. We have determined the crystal structure of a proteolytically stable fragment of SppABSK199A that has its C-terminal peptide bound in each of the eight active sites, creating a perfect circle of peptides. Substrate specificity pockets S1, S3, and S2' are identified and accommodate C-terminal residues Tyr331, Met329, and Tyr333, respectively. Tyr331 at the P1 position is conserved among most Bacillus species. The structure reveals that the C-terminus binds within the substrate-binding grooves in an antiparallel beta-sheet fashion. We show, by C-terminal truncations, that the C-terminus is not essential for oligomeric assembly. Kinetic analysis shows that a synthetic peptide corresponding to the C-terminus of SppABS competes with a fluorometric peptide substrate for the SppABS active site. A model is proposed for how the C-termini of SppA may function in the regulation of this membrane-bound self-compartmentalized protease. | ||
| - | + | Structure of signal peptide peptidase A with C-termini bound in the active sites: insights into specificity, self-processing, and regulation.,Nam SE, Paetzel M Biochemistry. 2013 Dec 10;52(49):8811-22. doi: 10.1021/bi4011489. Epub 2013 Nov, 25. PMID:24228759<ref>PMID:24228759</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bacsu]] | [[Category: Bacsu]] | ||
| - | [[Category: Nam, S E | + | [[Category: Nam, S E]] |
| - | [[Category: Paetzel, M | + | [[Category: Paetzel, M]] |
[[Category: Alpha/beta protein fold]] | [[Category: Alpha/beta protein fold]] | ||
[[Category: Bacterial cell membrane]] | [[Category: Bacterial cell membrane]] | ||
Revision as of 21:13, 24 December 2014
Structure of signal peptide peptidase A with C-termini bound in the active sites: insights into specificity, self-processing and regulation
| |||||||||||
