6WB3

Crystal structure of coiled coil region of human septin 4

6WB3 の概要

• エントリーDOI: 10.2210/pdb6wb3/pdb
• 分子名称: Septin-4, SULFATE ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: coiled coil, septin, structural protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8061.30

構造登録者

Cabrejos, D.A.L.,Cavini, I.,Sala, F.A.,Valadares, N.F.,Pereira, H.M.,Brandao-Neto, J.,Nascimento, A.F.Z.,Uson, I.,Araujo, A.P.U.,Garratt, R.C. (登録日: 2020-03-26, 公開日: 2021-03-17, 最終更新日: 2024-11-13)

主引用文献

Leonardo, D.A.,Cavini, I.A.,Sala, F.A.,Mendonca, D.C.,Rosa, H.V.D.,Kumagai, P.S.,Crusca Jr., E.,Valadares, N.F.,Marques, I.A.,Brandao-Neto, J.,Munte, C.E.,Kalbitzer, H.R.,Soler, N.,Uson, I.,Andre, I.,Araujo, A.P.U.,D'Muniz Pereira, H.,Garratt, R.C.
Orientational Ambiguity in Septin Coiled Coils and its Structural Basis.
J.Mol.Biol., 433:166889-166889, 2021

PubMed Abstract: Septins are an example of subtle molecular recognition whereby different paralogues must correctly assemble into functional filaments important for essential cellular events such as cytokinesis. Most possess C-terminal domains capable of forming coiled coils which are believed to be involved in filament formation and bundling. Here, we report an integrated structural approach which aims to unravel their architectural diversity and in so doing provide direct structural information for the coiled-coil regions of five human septins. Unexpectedly, we encounter dimeric structures presenting both parallel and antiparallel arrangements which are in consonance with molecular modelling suggesting that both are energetically accessible. These sequences therefore code for two metastable states of different orientations which employ different but overlapping interfaces. The antiparallel structures present a mixed coiled-coil interface, one side of which is dominated by a continuous chain of core hydrophilic residues. This unusual type of coiled coil could be used to expand the toolkit currently available to the protein engineer for the design of previously unforeseen coiled-coil based assemblies. Within a physiological context, our data provide the first atomic details related to the assumption that the parallel orientation is likely formed between septin monomers from the same filament whilst antiparallelism may participate in the widely described interfilament cross bridges necessary for higher order structures and thereby septin function.

PubMed: 33639214
DOI: 10.1016/j.jmb.2021.166889

実験手法

X-RAY DIFFRACTION (1.35 Å)