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| | ==Structure of signal peptide peptidase A with C-termini bound in the active sites: insights into specificity, self-processing and regulation== | | ==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=''> | + | <StructureSection load='4kwb' size='340' side='right'caption='[[4kwb]], [[Resolution|resolution]] 2.39Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <table><tr><td colspan='2'>[[4kwb]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4KWB FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kwb OCA], [https://pdbe.org/4kwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kwb RCSB], [https://www.ebi.ac.uk/pdbsum/4kwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kwb ProSAT]</span></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>
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| - | <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://pdbe.org/4kwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kwb RCSB], [http://www.ebi.ac.uk/pdbsum/4kwb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kwb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Nam, S E]] | + | [[Category: Large Structures]] |
| - | [[Category: Paetzel, M]] | + | [[Category: Nam SE]] |
| - | [[Category: Alpha/beta protein fold]] | + | [[Category: Paetzel M]] |
| - | [[Category: Bacterial cell membrane]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Self-compartmentalized]]
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| - | [[Category: Signal peptide digestion]]
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| Structural highlights
Function
SPPA_BACSU Digestion of cleaved signal peptides (By similarity). Required for efficient processing of precursors under conditions of hyper-secretion.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nam SE, Paetzel M. Structure of signal peptide peptidase A with C-termini bound in the active sites: insights into specificity, self-processing, and regulation. Biochemistry. 2013 Dec 10;52(49):8811-22. doi: 10.1021/bi4011489. Epub 2013 Nov, 25. PMID:24228759 doi:http://dx.doi.org/10.1021/bi4011489
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