3IMO

Structure from the mobile metagenome of Vibrio cholerae. Integron cassette protein VCH_CASS14

3IMO の概要

• エントリーDOI: 10.2210/pdb3imo/pdb
• 分子名称: Integron cassette protein, ACETATE ION (3 entities in total)
• 機能のキーワード: novel, integron protein, vibrio cholerae, argentinean o139 strain, unknown function
• 由来する生物種: Vibrio cholerae O139
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 59088.80

構造登録者

Deshpande, C.N.,Sureshan, V.,Harrop, S.J.,Boucher, Y.,Stokes, H.W.,Curmi, P.M.G.,Mabbutt, B.C. (登録日: 2009-08-11, 公開日: 2009-08-25, 最終更新日: 2024-04-03)

主引用文献

Sureshan, V.,Deshpande, C.N.,Boucher, Y.,Koenig, J.E.,Stokes, H.W.,Harrop, S.J.,Curmi, P.M.G.,Mabbutt, B.C.
Integron gene cassettes: a repository of novel protein folds with distinct interaction sites
Plos One, 8:e52934-e52934, 2013

PubMed Abstract: Mobile gene cassettes captured within integron arrays encompass a vast and diverse pool of genetic novelty. In most cases, functional annotation of gene cassettes directly recovered by cassette-PCR is obscured by their characteristically high sequence novelty. This inhibits identification of those specific functions or biological features that might constitute preferential factors for lateral gene transfer via the integron system. A structural genomics approach incorporating x-ray crystallography has been utilised on a selection of cassettes to investigate evolutionary relationships hidden at the sequence level. Gene cassettes were accessed from marine sediments (pristine and contaminated sites), as well as a range of Vibrio spp. We present six crystal structures, a remarkably high proportion of our survey of soluble proteins, which were found to possess novel folds. These entirely new structures are diverse, encompassing all-α, α+β and α/β fold classes, and many contain clear binding pocket features for small molecule substrates. The new structures emphasise the large repertoire of protein families encoded within the integron cassette metagenome and which remain to be characterised. Oligomeric association is a notable recurring property common to these new integron-derived proteins. In some cases, the protein-protein contact sites utilised in homomeric assembly could instead form suitable contact points for heterogeneous regulator/activator proteins or domains. Such functional features are ideal for a flexible molecular componentry needed to ensure responsive and adaptive bacterial functions.

PubMed: 23349695
DOI: 10.1371/journal.pone.0052934

実験手法

X-RAY DIFFRACTION (1.8 Å)