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1s2j

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Revision as of 06:42, 8 March 2018

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

Structural highlights

1s2j is a 2 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	PGRP-SA (DROME)
Activity:	Muramoyltetrapeptide carboxypeptidase, with EC number 3.4.17.13
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[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.

Publication Abstract from PubMed

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.

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Michel T, Reichhart JM, Hoffmann JA, Royet J. Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein. Nature. 2001 Dec 13;414(6865):756-9. PMID:11742401 doi:http://dx.doi.org/10.1038/414756a
↑ Gobert V, Gottar M, Matskevich AA, Rutschmann S, Royet J, Belvin M, Hoffmann JA, Ferrandon D. Dual activation of the Drosophila toll pathway by two pattern recognition receptors. Science. 2003 Dec 19;302(5653):2126-30. PMID:14684822 doi:http://dx.doi.org/10.1126/science.1085432
↑ Pili-Floury S, Leulier F, Takahashi K, Saigo K, Samain E, Ueda R, Lemaitre B. In vivo RNA interference analysis reveals an unexpected role for GNBP1 in the defense against Gram-positive bacterial infection in Drosophila adults. J Biol Chem. 2004 Mar 26;279(13):12848-53. Epub 2004 Jan 13. PMID:14722090 doi:http://dx.doi.org/10.1074/jbc.M313324200
↑ Bischoff V, Vignal C, Boneca IG, Michel T, Hoffmann JA, Royet J. Function of the drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria. Nat Immunol. 2004 Nov;5(11):1175-80. Epub 2004 Sep 26. PMID:15448690 doi:http://dx.doi.org/10.1038/ni1123
↑ Chang CI, Pili-Floury S, Herve M, Parquet C, Chelliah Y, Lemaitre B, Mengin-Lecreulx D, Deisenhofer J. A Drosophila pattern recognition receptor contains a peptidoglycan docking groove and unusual L,D-carboxypeptidase activity. PLoS Biol. 2004 Sep;2(9):E277. Epub 2004 Sep 7. PMID:15361936 doi:10.1371/journal.pbio.0020277

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1s2j"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Drosophila pattern-recognition receptor PGRP-SA==
 <StructureSection load='1s2j' size='340' side='right' caption='[[1s2j]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PGRP-SA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=1s2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s2j OCA], [http://pdbe.org/1s2j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s2j RCSB], [http://www.ebi.ac.uk/pdbsum/1s2j PDBsum]</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=1s2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s2j OCA], [http://pdbe.org/1s2j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s2j RCSB], [http://www.ebi.ac.uk/pdbsum/1s2j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s2j ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s2/1s2j_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s2/1s2j_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1s2j

From Proteopedia

Revision as of 06:42, 8 March 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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