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1sxr

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[[Image:1sxr.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sxr OCA], [http://www.ebi.ac.uk/pdbsum/1sxr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sxr RCSB]</span>
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'''Drosophila Peptidoglycan Recognition Protein (PGRP)-SA'''
'''Drosophila Peptidoglycan Recognition Protein (PGRP)-SA'''
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[[Category: Teyton, L.]]
[[Category: Teyton, L.]]
[[Category: Wilson, I A.]]
[[Category: Wilson, I A.]]
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[[Category: innate immunity]]
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[[Category: Innate immunity]]
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[[Category: pattern recognition receptor]]
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[[Category: Pattern recognition receptor]]
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[[Category: peptidoglycan]]
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[[Category: Peptidoglycan]]
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[[Category: toll pathway]]
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[[Category: Toll pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:15:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:48:28 2008''
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Revision as of 06:15, 3 May 2008

Template:STRUCTURE 1sxr

Drosophila Peptidoglycan Recognition Protein (PGRP)-SA


Overview

Peptidoglycan recognition proteins (PGRPs) form a recently discovered protein family, which is conserved from insect to mammals and is implicated in the innate immune system by interacting with/or degrading microbial peptidoglycans (PGNs). Drosophila PGRP-SA is a member of this family of pattern recognition receptors and is involved in insect Toll activation. We report here the crystal structure of PGRP-SA at 1.56 A resolution, which represents the first example of a "recognition" PGRP. Comparison with the catalytic Drosophila PGRP-LB reveals an overall structure conservation with an L-shaped hydrophilic groove that is likely the PGN carbohydrate core binding site, but further suggests some possible functional homology between recognition and catalytic PGRPs. Consistent with sequence analysis, PGRP-SA does not contain the canonical zinc-binding residues found in catalytic PGRPs. However, substitution of the zinc-binding cysteine residue by serine, along with an altered coordinating histidine residue, assembles a constellation of residues that resembles a modified catalytic triad. The serine/histidine juxtaposition to a threonine residue and a carbonyl oxygen atom, along with conservation of the catalytic water molecule found in PGRP-LB, tantalizingly suggests some hydrolytic function for this member of receptor PGRPs.

About this Structure

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

Reference

Crystal structure of the Drosophila peptidoglycan recognition protein (PGRP)-SA at 1.56 A resolution., Reiser JB, Teyton L, Wilson IA, J Mol Biol. 2004 Jul 16;340(4):909-17. PMID:15223330 Page seeded by OCA on Sat May 3 09:15:33 2008

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