5xz4
The X-tay structure of Bumblebee PGRP-SA
Structural highlights
FunctionPublication Abstract from PubMedThe peptidoglycan recognition protein SAs (PGRP-SAs) from Bombus ignitus (Bi-PGRP-SA), Apis mellifera (Am-PGRP-SA), and Megachile rotundata PGRP-SA (Mr-PGRP-SA) exhibit an intrinsic ability to preferentially bind to Dap-type peptidoglycan (PGN) from Bacillus subtilis rather than Lys-type PGN from Micrococcus luteus This ability is more analogous to the binding exhibited by PGRP-LCx and PGRP-SD than to that exhibited by PGRP-SA in Drosophila Moreover, Bi-PGRP-SA and Am-PGRP-SA share greater sequence identity with Drosophila PGRP-LCx than with PGRP-SD and retain several conserved contact residues, including His(37)/His(38), His(60)/His(61), Trp(66)/Trp(67), Ala(150)/Ala(151), and Thr(151)/Thr(152) However, the corresponding contact residue Arg(85) is not a major anchor residue in bees (e.g., bumblebees, honeybees, and leaf-cutting bees), and an in silico analysis indicated that the residues Thr(151)/Thr(152) and Ser(153)/Ser(154) of Bi-PGRP-SA and Am-PGRP-SA are deduced to be anchor residues. In addition, the nonconserved residues Asp(67) in Bi-PGRP-SA and Mr-PGRP-SA and His(68) in Am-PGRP-SA are deduced to be involved in the binding to Dap-type PGNs in bumblebees, honeybees, and leaf-cutting bees. We conclude that the structures and specificities of PGRP-SAs in bees are more analogous to those of PGRP-LCx than to those of Drosophila PGRP-SA. This phenomenon might be explained by the fact that the evolutionary clade of Hymenoptera is more ancient than that of Diptera. Structural Insights into the Preferential Binding of PGRP-SAs from Bumblebees and Honeybees to Dap-Type Peptidoglycans Rather than Lys-Type Peptidoglycans.,Liu Y, Zhao X, Huang J, Chen M, An J J Immunol. 2019 Jan 1;202(1):249-259. doi: 10.4049/jimmunol.1800439. Epub 2018, Dec 3. PMID:30510067[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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