1s2j: Difference between revisions

Revision as of 16:42, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1s2j.png

Template:STRUCTURE 1s2j

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

Template:ABSTRACT PUBMED 15361936

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

Page seeded by OCA on Mon Jul 28 16:42:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1s2j.jpg|left|200px]]
+{{Seed}}
+[[Image:1s2j.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1s2j|  PDB=1s2j  |  SCENE=  }}
-'''Crystal structure of the Drosophila pattern-recognition receptor PGRP-SA'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15361936}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15361936 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15361936}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Pili-Floury, S.]]
 [[Category: Mixed beta-sheet]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:13:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:42:00 2008''