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| | ==Legionella pneumophila LapG (EGTA-treated)== | | ==Legionella pneumophila LapG (EGTA-treated)== |
| - | <StructureSection load='4fgp' size='340' side='right' caption='[[4fgp]], [[Resolution|resolution]] 1.73Å' scene=''> | + | <StructureSection load='4fgp' size='340' side='right'caption='[[4fgp]], [[Resolution|resolution]] 1.73Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fgp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Legph Legph]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FGP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FGP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fgp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FGP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fgo|4fgo]], [[4fgq|4fgq]]</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]] 1.73Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpg0828 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272624 LEGPH])</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=4fgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fgp OCA], [https://pdbe.org/4fgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fgp RCSB], [https://www.ebi.ac.uk/pdbsum/4fgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fgp 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=4fgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fgp OCA], [http://pdbe.org/4fgp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fgp RCSB], [http://www.ebi.ac.uk/pdbsum/4fgp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fgp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q5ZXA4_LEGPH Q5ZXA4_LEGPH] |
| - | The bacterial dinucleotide second messenger c-di-GMP has emerged as a central molecule in regulating bacterial behavior, including motility and biofilm formation. Proteins for the synthesis and degradation of c-di-GMP and effectors for its signal transmission are widely used in the bacterial domain. Previous work established the GGDEF-EAL domain-containing receptor LapD as a central switch in Pseudomonas fluorescens cell adhesion. LapD senses c-di-GMP inside the cytosol and relays this signal to the outside by the differential recruitment of the periplasmic protease LapG. Here we identify the core components of an orthologous system in Legionella pneumophila. Despite only moderate sequence conservation at the protein level, key features concerning the regulation of LapG are retained. The output domain of the LapD-like receptor from L. pneumophila, CdgS9, binds the LapG ortholog involving a strictly conserved surface tryptophan residue. While the endogenous substrate for L. pneumophila LapG is unknown, the enzyme processed the corresponding P. fluorescens substrate, indicating a common catalytic mechanism and substrate recognition. Crystal structures of L. pneumophila LapG provide the first atomic models of bacterial proteases of the DUF920 family and reveal a conserved calcium-binding site important for LapG function.
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| - | Structural characterization of a conserved, calcium-dependent periplasmic protease from Legionella pneumophila.,Chatterjee D, Boyd CD, O'Toole GA, Sondermann H J Bacteriol. 2012 Aug;194(16):4415-25. doi: 10.1128/JB.00640-12. Epub 2012 Jun, 15. PMID:22707706<ref>PMID:22707706</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 4fgp" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Legph]] | + | [[Category: Large Structures]] |
| - | [[Category: Boyd, C D]] | + | [[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] |
| - | [[Category: Chatterjee, D]] | + | [[Category: Boyd CD]] |
| - | [[Category: Sondermann, H]] | + | [[Category: Chatterjee D]] |
| - | [[Category: Toole, G A.O]] | + | [[Category: O'Toole GA]] |
| - | [[Category: Calcium binding]] | + | [[Category: Sondermann H]] |
| - | [[Category: Duf920]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Protease]]
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