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2MK5

Solution structure of a protein domain

2MK5 の概要
エントリーDOI10.2210/pdb2mk5/pdb
関連するPDBエントリー4OLK 4OLS
NMR情報BMRB: 19752
分子名称Endolysin (1 entity in total)
機能のキーワードhydrolase
由来する生物種Staphylococcus phage GH15
タンパク質・核酸の鎖数1
化学式量合計14048.75
構造登録者
Feng, Y.,Gu, J. (登録日: 2014-01-24, 公開日: 2014-05-28, 最終更新日: 2024-05-01)
主引用文献Gu, J.,Feng, Y.,Feng, X.,Sun, C.,Lei, L.,Ding, W.,Niu, F.,Jiao, L.,Yang, M.,Li, Y.,Liu, X.,Song, J.,Cui, Z.,Han, D.,Du, C.,Yang, Y.,Ouyang, S.,Liu, Z.J.,Han, W.
Structural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin.
Plos Pathog., 10:e1004109-e1004109, 2014
Cited by
PubMed Abstract: The lysin LysGH15, which is derived from the staphylococcal phage GH15, demonstrates a wide lytic spectrum and strong lytic activity against methicillin-resistant Staphylococcus aureus (MRSA). Here, we find that the lytic activity of the full-length LysGH15 and its CHAP domain is dependent on calcium ions. To elucidate the molecular mechanism, the structures of three individual domains of LysGH15 were determined. Unexpectedly, the crystal structure of the LysGH15 CHAP domain reveals an "EF-hand-like" calcium-binding site near the Cys-His-Glu-Asn quartet active site groove. To date, the calcium-binding site in the LysGH15 CHAP domain is unique among homologous proteins, and it represents the first reported calcium-binding site in the CHAP family. More importantly, the calcium ion plays an important role as a switch that modulates the CHAP domain between the active and inactive states. Structure-guided mutagenesis of the amidase-2 domain reveals that both the zinc ion and E282 are required in catalysis and enable us to propose a catalytic mechanism. Nuclear magnetic resonance (NMR) spectroscopy and titration-guided mutagenesis identify residues (e.g., N404, Y406, G407, and T408) in the SH3b domain that are involved in the interactions with the substrate. To the best of our knowledge, our results constitute the first structural information on the biochemical features of a staphylococcal phage lysin and represent a pivotal step forward in understanding this type of lysin.
PubMed: 24831957
DOI: 10.1371/journal.ppat.1004109
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2mk5
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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