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| - | [[Image:3bf0.jpg|left|200px]] | |
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| - | {{Structure
| + | ==Crystal structure of Escherichia coli Signal peptide peptidase (SppA), Native crystals== |
| - | |PDB= 3bf0 |SIZE=350|CAPTION= <scene name='initialview01'>3bf0</scene>, resolution 2.550Å
| + | <StructureSection load='3bf0' size='340' side='right'caption='[[3bf0]], [[Resolution|resolution]] 2.55Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[3bf0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BF0 FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55Å</td></tr> |
| - | |GENE= sppA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bf0 OCA], [https://pdbe.org/3bf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bf0 RCSB], [https://www.ebi.ac.uk/pdbsum/3bf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bf0 ProSAT]</span></td></tr> |
| - | |DOMAIN=
| + | </table> |
| - | |RELATEDENTRY=[[3bez|3BEZ]] | + | == Function == |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bf0 OCA], [http://www.ebi.ac.uk/pdbsum/3bf0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bf0 RCSB]</span>
| + | [https://www.uniprot.org/uniprot/SPPA_ECOLI SPPA_ECOLI] Digests cleaved signal peptides in vitro, its in vivo function is unknown. This activity is necessary to maintain proper secretion of mature proteins across the membrane.<ref>PMID:3522590</ref> <ref>PMID:18476724</ref> <ref>PMID:21810987</ref> <ref>PMID:18164727</ref> |
| - | }}
| + | == Evolutionary Conservation == |
| - | | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | '''Crystal structure of Escherichia coli Signal peptide peptidase (SppA), Native crystals'''
| + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/3bf0_consurf.spt"</scriptWhenChecked> |
| - | ==Overview== | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | Signal peptide peptidase (Spp) is the enzyme responsible for cleaving the remnant signal peptides left behind in the membrane following Sec-dependent protein secretion. Spp activity appears to be present in all cell types, eukaryotic, prokaryotic and archaeal. Here we report the first structure of a signal peptide peptidase, that of the Escherichia coli SppA (SppA(EC)). SppA(EC) forms a tetrameric assembly with a novel bowl-shaped architecture. The bowl has a dramatically hydrophobic interior and contains four separate active sites that utilize a Ser/Lys catalytic dyad mechanism. Our structural analysis of SppA reveals that while in many Gram-negative bacteria as well as characterized plant variants, a tandem duplication in the protein fold creates an intact active site at the interface between the repeated domains, other species, particularly Gram-positive and archaeal organisms, encode half-size, unduplicated SppA variants that could form similar oligomers to their duplicated counterparts, but using an octamer arrangement and with the catalytic residues provided by neighboring monomers. The structure reveals a similarity in the protein fold between the domains in the periplasmic Ser/Lys protease SppA and the monomers seen in the cytoplasmic Ser/His/Asp protease ClpP. We propose that SppA may, in addition to its role in signal peptide hydrolysis, have a role in the quality assurance of periplasmic and membrane-bound proteins, similar to the role that ClpP plays for cytoplasmic proteins.
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | | + | </jmolCheckbox> |
| - | ==About this Structure== | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bf0 ConSurf]. |
| - | 3BF0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BF0 OCA].
| + | <div style="clear:both"></div> |
| - | | + | == References == |
| - | ==Reference== | + | <references/> |
| - | Crystal structure of a bacterial signal Peptide peptidase., Kim AC, Oliver DC, Paetzel M, J Mol Biol. 2008 Feb 15;376(2):352-66. Epub 2007 Dec 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18164727 18164727]
| + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Paetzel, M.]] | + | [[Category: Paetzel M]] |
| - | [[Category: bacterial]]
| + | |
| - | [[Category: hydrolase]]
| + | |
| - | [[Category: inner membrane]]
| + | |
| - | [[Category: membrane]]
| + | |
| - | [[Category: protease]]
| + | |
| - | [[Category: ser/lys protease]]
| + | |
| - | [[Category: transmembrane]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:25:41 2008''
| + | |
| Structural highlights
Function
SPPA_ECOLI Digests cleaved signal peptides in vitro, its in vivo function is unknown. This activity is necessary to maintain proper secretion of mature proteins across the membrane.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Ichihara S, Suzuki T, Suzuki M, Mizushima S. Molecular cloning and sequencing of the sppA gene and characterization of the encoded protease IV, a signal peptide peptidase, of Escherichia coli. J Biol Chem. 1986 Jul 15;261(20):9405-11. PMID:3522590
- ↑ Wang P, Shim E, Cravatt B, Jacobsen R, Schoeniger J, Kim AC, Paetzel M, Dalbey RE. Escherichia coli signal peptide peptidase A is a serine-lysine protease with a lysine recruited to the nonconserved amino-terminal domain in the S49 protease family. Biochemistry. 2008 Jun 17;47(24):6361-9. doi: 10.1021/bi800657p. Epub 2008 May, 14. PMID:18476724 doi:http://dx.doi.org/10.1021/bi800657p
- ↑ Saito A, Hizukuri Y, Matsuo E, Chiba S, Mori H, Nishimura O, Ito K, Akiyama Y. Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria. Proc Natl Acad Sci U S A. 2011 Aug 16;108(33):13740-5. doi:, 10.1073/pnas.1108376108. Epub 2011 Aug 2. PMID:21810987 doi:http://dx.doi.org/10.1073/pnas.1108376108
- ↑ Kim AC, Oliver DC, Paetzel M. Crystal structure of a bacterial signal Peptide peptidase. J Mol Biol. 2008 Feb 15;376(2):352-66. Epub 2007 Dec 4. PMID:18164727 doi:10.1016/j.jmb.2007.11.080
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