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| | ==Structure of a PDZ-protease bound to a substrate-binding adaptor== | | ==Structure of a PDZ-protease bound to a substrate-binding adaptor== |
| - | <StructureSection load='5wql' size='340' side='right' caption='[[5wql]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5wql' size='340' side='right'caption='[[5wql]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wql]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WQL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wql]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WQL FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nlpI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), prc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/C-terminal_processing_peptidase C-terminal processing peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.102 3.4.21.102] </span></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=5wql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wql OCA], [https://pdbe.org/5wql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wql RCSB], [https://www.ebi.ac.uk/pdbsum/5wql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wql ProSAT]</span></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=5wql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wql OCA], [http://pdbe.org/5wql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wql RCSB], [http://www.ebi.ac.uk/pdbsum/5wql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wql ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NLPI_ECOLI NLPI_ECOLI]] May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA).<ref>PMID:10400590</ref> <ref>PMID:20833130</ref> [[http://www.uniprot.org/uniprot/PRC_ECOLI PRC_ECOLI]] Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses. | + | [https://www.uniprot.org/uniprot/NLPI_ECOLI NLPI_ECOLI] May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA).<ref>PMID:10400590</ref> <ref>PMID:20833130</ref> |
| | <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: C-terminal processing peptidase]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Ecoli]] | + | [[Category: Large Structures]] |
| - | [[Category: Chang, C I]] | + | [[Category: Chang CI]] |
| - | [[Category: Su, M Y]] | + | [[Category: Su MY]] |
| - | [[Category: Nlpi]]
| + | |
| - | [[Category: Peptidoglycan]]
| + | |
| - | [[Category: Prc]]
| + | |
| - | [[Category: Protein binding-signaling protein-hydrolase-peptide complex]]
| + | |
| - | [[Category: Protein degradation]]
| + | |
| Structural highlights
Function
NLPI_ECOLI May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA).[1] [2]
Publication Abstract from PubMed
Peptidoglycan (PG) is a highly cross-linked, protective mesh-like sacculus that surrounds the bacterial cytoplasmic membrane. Expansion of PG is tightly coupled to growth of a bacterial cell and requires hydrolases to cleave the cross-links for insertion of nascent PG material. In Escherichia coli, a proteolytic system comprising the periplasmic PDZ-protease Prc and the lipoprotein adaptor NlpI contributes to PG enlargement by regulating cellular levels of MepS, a cross-link-specific hydrolase. Here, we demonstrate how NlpI binds Prc to facilitate the degradation of its substrate MepS by structural and mutational analyses. An NlpI homodimer binds two molecules of Prc and forms three-sided MepS-docking cradles using its tetratricopeptide repeats. Prc forms a monomeric bowl-shaped structure with a lid-like PDZ domain connected by a substrate-sensing hinge that recognizes the bound C terminus of the substrate. In summary, our study reveals mechanistic details of protein degradation by the PDZ-protease Prc bound to its cognate adaptor protein.
Structural basis of adaptor-mediated protein degradation by the tail-specific PDZ-protease Prc.,Su MY, Som N, Wu CY, Su SC, Kuo YT, Ke LC, Ho MR, Tzeng SR, Teng CH, Mengin-Lecreulx D, Reddy M, Chang CI Nat Commun. 2017 Nov 15;8(1):1516. doi: 10.1038/s41467-017-01697-9. PMID:29138488[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ohara M, Wu HC, Sankaran K, Rick PD. Identification and characterization of a new lipoprotein, NlpI, in Escherichia coli K-12. J Bacteriol. 1999 Jul;181(14):4318-25. PMID:10400590
- ↑ Sanchez-Torres V, Maeda T, Wood TK. Global regulator H-NS and lipoprotein NlpI influence production of extracellular DNA in Escherichia coli. Biochem Biophys Res Commun. 2010 Oct 15;401(2):197-202. doi:, 10.1016/j.bbrc.2010.09.026. Epub 2010 Sep 15. PMID:20833130 doi:http://dx.doi.org/10.1016/j.bbrc.2010.09.026
- ↑ Su MY, Som N, Wu CY, Su SC, Kuo YT, Ke LC, Ho MR, Tzeng SR, Teng CH, Mengin-Lecreulx D, Reddy M, Chang CI. Structural basis of adaptor-mediated protein degradation by the tail-specific PDZ-protease Prc. Nat Commun. 2017 Nov 15;8(1):1516. doi: 10.1038/s41467-017-01697-9. PMID:29138488 doi:http://dx.doi.org/10.1038/s41467-017-01697-9
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