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7BT8

Mevo lectin complex with mannotriose

7BT8 の概要
エントリーDOI10.2210/pdb7bt8/pdb
分子名称lectin, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose, 1,2-ETHANEDIOL, ... (5 entities in total)
機能のキーワードbeta-prism i fold lectin, archeal lectin, heptamer, ring shape structure, sugar binding protein
由来する生物種Methanococcus voltae (strain ATCC BAA-1334 / A3)
タンパク質・核酸の鎖数7
化学式量合計108907.14
構造登録者
Sivaji, N.,Suguna, K.,Surolia, A.,Vijayan, M. (登録日: 2020-03-31, 公開日: 2021-02-03, 最終更新日: 2023-11-29)
主引用文献Sivaji, N.,Suguna, K.,Surolia, A.,Vijayan, M.
Structural and related studies on Mevo lectin from Methanococcus voltae A3: the first thorough characterization of an archeal lectin and its interactions.
Glycobiology, 31:315-328, 2021
Cited by
PubMed Abstract: Crystallographic and solution studies of Mevo lectin and its complexes, the first effort of its kind on an archeal lectin, reveal a structure similar to β-prism I fold lectins from plant and animal sources, but with a quaternary association involving a ring structure with seven-fold symmetry. Each subunit in the heptamer carries one sugar binding site on the first Greek key motif. The oligomeric interface is primarily made up of a parallel β-sheet involving a strand of Greek key I of one subunit and Greek key ΙΙΙ from a neighboring subunit. The crystal structures of the complexes of the lectin with mannose, αMan(1,2)αMan, αMan(1,3)αMan, a mannotriose and a mannopentose revealed a primary binding site similar to that found in other mannose specific β-prism I fold lectins. The complex with αMan(1,3)αMan provides an interesting case in which a few subunits have the reducing end at the primary binding site, while the majority have the nonreducing end at the primary binding site. The structures of complexes involving the trisaccharide and the pentasaccharide exhibit cross-linking among heptameric molecules. The observed arrangements may be relevant to the multivalency of the lectin. Phylogenetic analysis of amino acid sequences indicates that Mevo lectin is closer to β-prism I fold animal lectins than with those of plant origin. The results presented here reinforce the conclusion regarding the existence of lectins in all three domains of life. It would also appear that lectins evolved to the present form before the three domains diverged.
PubMed: 32651948
DOI: 10.1093/glycob/cwaa063
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.7 Å)
構造検証レポート
Validation report summary of 7bt8
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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