1s2j: Difference between revisions

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[[Image:1s2j.jpg|left|200px]]<br /><applet load="1s2j" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1s2j.jpg|left|200px]]
caption="1s2j, resolution 2.20&Aring;" />
 
'''Crystal structure of the Drosophila pattern-recognition receptor PGRP-SA'''<br />
{{Structure
|PDB= 1s2j |SIZE=350|CAPTION= <scene name='initialview01'>1s2j</scene>, resolution 2.20&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
|ACTIVITY= [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]
|GENE= PGRP-SA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])
}}
 
'''Crystal structure of the Drosophila pattern-recognition receptor PGRP-SA'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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 <scene name='pdbligand=PO4:'>PO4</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2J OCA].  
1S2J is a [[Single protein]] structure of sequence from [http://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].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15361936 15361936]
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://www.ncbi.nlm.nih.gov/pubmed/15361936 15361936]
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Muramoyltetrapeptide carboxypeptidase]]
[[Category: Muramoyltetrapeptide carboxypeptidase]]
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[[Category: pi-helix (one turn)]]
[[Category: pi-helix (one turn)]]


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Revision as of 14:59, 20 March 2008

File:1s2j.jpg


PDB ID 1s2j

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands:
Gene: PGRP-SA (Drosophila melanogaster)
Activity: Muramoyltetrapeptide carboxypeptidase, with EC number 3.4.17.13
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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

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