1s2j

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[[Image:1s2j.jpg|left|200px]]
[[Image:1s2j.jpg|left|200px]]
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{{Structure
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|PDB= 1s2j |SIZE=350|CAPTION= <scene name='initialview01'>1s2j</scene>, resolution 2.20&Aring;
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The line below this paragraph, containing "STRUCTURE_1s2j", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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|GENE= PGRP-SA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])
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|DOMAIN=
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{{STRUCTURE_1s2j| PDB=1s2j | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1s2j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s2j RCSB]</span>
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'''Crystal structure of the Drosophila pattern-recognition receptor PGRP-SA'''
'''Crystal structure of the Drosophila pattern-recognition receptor PGRP-SA'''
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[[Category: Mengin-Lecreulx, D.]]
[[Category: Mengin-Lecreulx, D.]]
[[Category: Pili-Floury, S.]]
[[Category: Pili-Floury, S.]]
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[[Category: mixed beta-sheet]]
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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://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:13:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:36:29 2008''
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Revision as of 05:13, 3 May 2008

Template:STRUCTURE 1s2j

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


Overview

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.

About this Structure

1S2J is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 08:13:02 2008

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