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Crystal structure of the Drosophila peptidoglycan recognition protein (PGRP)-SA at 1.56 A resolution.

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Reiser JB,Teyton L,Wilson IA

doi

10.1016/j.jmb.2004.04.077

keywords:

subject

Has Abstract

pub_date

2004-07-16 00:00:00

pages

909-17

issue

4

eissn

0022-2836

issn

1089-8638

pii

S002228360400470X

journal_volume

340

pub_type

杂志文章

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