5XZ4

The X-tay structure of Bumblebee PGRP-SA

5XZ4 の概要

• エントリーDOI: 10.2210/pdb5xz4/pdb
• 分子名称: Bumblebee peptidoglycan recognition protein SA, SULFATE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: bumblebee, pgrp-sa, immune system
• 由来する生物種: Bombus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38963.98

構造登録者

Liu, Y.J.,Huang, J.X.,Zhao, X.M.,An, J.D. (登録日: 2017-07-11, 公開日: 2018-09-19, 最終更新日: 2024-11-06)

主引用文献

Liu, Y.J.,Zhao, X.M.,Huang, J.X.,Chen, M.M.,An, J.D.
Structural Insights into the Preferential Binding of PGRP-SAs from Bumblebees and Honeybees to Dap-Type Peptidoglycans Rather than Lys-Type Peptidoglycans.
J Immunol., 202:249-259, 2019

PubMed Abstract: The peptidoglycan recognition protein SAs (PGRP-SAs) from (Bi-PGRP-SA), (Am-PGRP-SA), and PGRP-SA (Mr-PGRP-SA) exhibit an intrinsic ability to preferentially bind to Dap-type peptidoglycan (PGN) from rather than Lys-type PGN from This ability is more analogous to the binding exhibited by PGRP-LCx and PGRP-SD than to that exhibited by PGRP-SA in Moreover, Bi-PGRP-SA and Am-PGRP-SA share greater sequence identity with PGRP-LCx than with PGRP-SD and retain several conserved contact residues, including His/His, His/His, Trp/Trp, Ala/Ala, and Thr/Thr However, the corresponding contact residue Arg 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/Thr and Ser/Ser of Bi-PGRP-SA and Am-PGRP-SA are deduced to be anchor residues. In addition, the nonconserved residues Asp in Bi-PGRP-SA and Mr-PGRP-SA and His 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 PGRP-SA. This phenomenon might be explained by the fact that the evolutionary clade of Hymenoptera is more ancient than that of Diptera.

PubMed: 30510067
DOI: 10.4049/jimmunol.1800439

実験手法

X-RAY DIFFRACTION (1.41 Å)