7BK7

PfCopC mutant - D83N

これはPDB形式変換不可エントリーです。

7BK7 の概要

• エントリーDOI: 10.2210/pdb7bk7/pdb
• 関連するPDBエントリー: 7BK5 7BK6
• 分子名称: Putative copper resistance protein, ACETATE ION, COPPER (II) ION, ... (6 entities in total)
• 機能のキーワード: copper binding, copper transport, metal binding protein
• 由来する生物種: Pseudomonas fluorescens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20602.68

構造登録者

Muderspach, S.J.,Ipsen, J.,Rollan, C.H.,Bertelsen, A.B.,Norholm, M.H.H.,Johansen, K.S.,Lo Leggio, L. (登録日: 2021-01-15, 公開日: 2021-07-07, 最終更新日: 2024-01-31)

主引用文献

Ipsen, J.O.,Hernandez-Rollan, C.,Muderspach, S.J.,Brander, S.,Bertelsen, A.B.,Jensen, P.E.,Norholm, M.H.H.,Lo Leggio, L.,Johansen, K.S.
Copper binding and reactivity at the histidine brace motif: insights from mutational analysis of the Pseudomonas fluorescens copper chaperone CopC.
Febs Lett., 595:1708-1720, 2021

PubMed Abstract: The histidine brace (His-brace) is a copper-binding motif that is associated with both oxidative enzymes and proteinaceous copper chaperones. Here, we used biochemical and structural methods to characterize mutants of a His-brace-containing copper chaperone from Pseudomonas fluorescens (PfCopC). A total of 15 amino acid variants in primary and second-sphere residues were produced and characterized in terms of their copper binding and redox properties. PfCopC has a very high affinity for Cu(II) and also binds Cu(I). A high reorganization barrier likely prevents redox cycling and, thus, catalysis. In contrast, mutations in the conserved second-sphere Glu27 enable slow oxidation of ascorbate. The crystal structure of the variant E27A confirmed copper binding at the His-brace. Unexpectedly, Asp83 at the equatorial position was shown to be indispensable for Cu(II) binding in the His-brace of PfCopC. A PfCopC mutant that was designed to mimic the His-brace from lytic polysaccharide monooxygenase-like family X325 did not bind Cu(II), but was still able to bind Cu(I). These results highlight the importance of the proteinaceous environment around the copper His-brace for reactivity and, thus, the difference between enzyme and chaperone.

PubMed: 33896006
DOI: 10.1002/1873-3468.14092

実験手法

X-RAY DIFFRACTION (2.3 Å)