Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

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

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Reiser, J. B.
  • Teyton, Luc
  • Wilson, Ian

publication date

  • July 2004

journal

  • Journal of Molecular Biology  Journal

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.

subject areas

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carrier Proteins
  • Conserved Sequence
  • Crystallography, X-Ray
  • Drosophila
  • Drosophila Proteins
  • Histidine
  • Models, Molecular
  • Molecular Sequence Data
  • Oxygen
  • Protein Structure, Secondary
  • Sequence Homology, Amino Acid
  • Serine
  • Water
  • X-Ray Diffraction
scroll to property group menus

Research

keywords

  • Toll pathway
  • innate immunity
  • pattern recognition receptor
  • serine hydrolase
  • zinc hydrolase
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2004.04.077

PubMed ID

  • 15223330
scroll to property group menus

Additional Document Info

start page

  • 909

end page

  • 917

volume

  • 340

issue

  • 4

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support