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1s2j

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(New page: 200px<br /><applet load="1s2j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s2j, resolution 2.20&Aring;" /> '''Crystal structure of...)
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[[Image:1s2j.jpg|left|200px]]<br /><applet load="1s2j" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1s2j, resolution 2.20&Aring;" />
 
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'''Crystal structure of the Drosophila pattern-recognition receptor PGRP-SA'''<br />
 
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==Overview==
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==Crystal structure of the Drosophila pattern-recognition receptor PGRP-SA==
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The Drosophila peptidoglycan recognition protein SA (PGRP-SA) is, critically involved in sensing bacterial infection and activating the Toll, signaling pathway, which induces the expression of specific antimicrobial, peptide genes. We have determined the crystal structure of PGRP-SA to, 2.2-A resolution and analyzed its peptidoglycan (PG) recognition and, signaling activities. We found an extended surface groove in the structure, of PGRP-SA, lined with residues that are highly diverse among different, PGRPs. Mutational analysis identified it as a PG docking groove required, for Toll signaling and showed that residue Ser158 is essential for both PG, binding and Toll activation. Contrary to the general belief that PGRP-SA, has lost enzyme function and serves primarily for PG sensing, we found, that it possesses an intrinsic L,D-carboxypeptidase activity for, diaminopimelic acid-type tetrapeptide PG fragments but not lysine-type PG, fragments, and that Ser158 and His42 may participate in the hydrolytic, activity. As L,D-configured peptide bonds exist only in prokaryotes, this, work reveals a rare enzymatic activity in a eukaryotic protein known for, sensing bacteria and provides a possible explanation of how PGRP-SA, mediates Toll activation specifically in response to lysine-type PG.
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<StructureSection load='1s2j' size='340' side='right'caption='[[1s2j]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1s2j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S2J FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s2j OCA], [https://pdbe.org/1s2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s2j RCSB], [https://www.ebi.ac.uk/pdbsum/1s2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s2j ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PGPSA_DROME PGPSA_DROME] Peptidoglycan-recognition protein that plays a key role in innate immnunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway. Has no activity against on Gram-negative bacteria and fungi. Shows some partial redundancy with PRPGP-SD in Gram-positive bacteria recognition. May act by forming a complex with GNBP1 that activates the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway. Binds to diaminopimelic acid-type tetrapeptide PGN (DAP-type PGN) and lysine-type PGN (Lys-type PGN). Has some L,D-carboxypeptidase activity for DAP-type PGN, which are specific to prokaryotes, but not for Lys-type PGN.<ref>PMID:11742401</ref> <ref>PMID:14684822</ref> <ref>PMID:14722090</ref> <ref>PMID:15448690</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s2/1s2j_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1s2j ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Drosophila peptidoglycan recognition protein SA (PGRP-SA) is critically involved in sensing bacterial infection and activating the Toll signaling pathway, which induces the expression of specific antimicrobial peptide genes. We have determined the crystal structure of PGRP-SA to 2.2-A resolution and analyzed its peptidoglycan (PG) recognition and signaling activities. We found an extended surface groove in the structure of PGRP-SA, lined with residues that are highly diverse among different PGRPs. Mutational analysis identified it as a PG docking groove required for Toll signaling and showed that residue Ser158 is essential for both PG binding and Toll activation. Contrary to the general belief that PGRP-SA has lost enzyme function and serves primarily for PG sensing, we found that it possesses an intrinsic L,D-carboxypeptidase activity for diaminopimelic acid-type tetrapeptide PG fragments but not lysine-type PG fragments, and that Ser158 and His42 may participate in the hydrolytic activity. As L,D-configured peptide bonds exist only in prokaryotes, this work reveals a rare enzymatic activity in a eukaryotic protein known for sensing bacteria and provides a possible explanation of how PGRP-SA mediates Toll activation specifically in response to lysine-type PG.
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==About this Structure==
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A Drosophila pattern recognition receptor contains a peptidoglycan docking groove and unusual L,D-carboxypeptidase activity.,Chang CI, Pili-Floury S, Herve M, Parquet C, Chelliah Y, Lemaitre B, Mengin-Lecreulx D, Deisenhofer J PLoS Biol. 2004 Sep;2(9):E277. Epub 2004 Sep 7. PMID:15361936<ref>PMID:15361936</ref>
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1S2J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Muramoyltetrapeptide_carboxypeptidase Muramoyltetrapeptide carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.13 3.4.17.13] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S2J OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A Drosophila pattern recognition receptor contains a peptidoglycan docking groove and unusual L,D-carboxypeptidase activity., Chang CI, Pili-Floury S, Herve M, Parquet C, Chelliah Y, Lemaitre B, Mengin-Lecreulx D, Deisenhofer J, PLoS Biol. 2004 Sep;2(9):E277. Epub 2004 Sep 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15361936 15361936]
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</div>
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<div class="pdbe-citations 1s2j" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
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[[Category: Muramoyltetrapeptide carboxypeptidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chang C-I]]
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[[Category: Chang, C.I.]]
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[[Category: Chelliah Y]]
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[[Category: Chelliah, Y.]]
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[[Category: Deisenhofer J]]
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[[Category: Deisenhofer, J.]]
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[[Category: Lemaitre B]]
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[[Category: Lemaitre, B.]]
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[[Category: Mengin-Lecreulx D]]
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[[Category: Mengin-Lecreulx, D.]]
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[[Category: Pili-Floury S]]
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[[Category: Pili-Floury, S.]]
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[[Category: PO4]]
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[[Category: mixed beta-sheet]]
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[[Category: pi-helix (one turn)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:03:10 2007''
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Current revision

Crystal structure of the Drosophila pattern-recognition receptor PGRP-SA

PDB ID 1s2j

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