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PDBsum entry 3fuy
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Structural genomics, unknown function
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PDB id
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3fuy
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PDB id:
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| Name: |
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Structural genomics, unknown function
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Title:
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Structure from the mobile metagenome of cole harbour salt marsh: integron cassette protein hfx_cass1
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Structure:
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Putative integron gene cassette protein. Chain: a, b, c. Synonym: hfx_cass1. Engineered: yes
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Source:
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Uncultured bacterium. Organism_taxid: 77133. Gene: orf1. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.00Å
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R-factor:
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0.199
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R-free:
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0.234
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Authors:
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V.Sureshan,C.N.Deshpande,S.J.Harrop,M.Kudrytska,J.E.Koenig, E.Evdokimova,J.Osipiuk,A.Edwards,A.Savchenko,A.Joachimiak, W.F.Doolittle,H.W.Stokes,P.M.G.Curmi,B.C.Mabbutt,Midwest Center For Structural Genomics (Mcsg)
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Key ref:
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V.Sureshan
et al.
(2013).
Integron gene cassettes: a repository of novel protein folds with distinct interaction sites.
Plos One,
8,
e52934.
PubMed id:
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Date:
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15-Jan-09
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Release date:
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24-Feb-09
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PROCHECK
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Headers
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References
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B0BGB0
(B0BGB0_9BACT) -
Putative integron gene cassette protein from uncultured bacterium
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Seq: Struc:
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158 a.a.
156 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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Plos One
8:e52934
(2013)
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PubMed id:
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Integron gene cassettes: a repository of novel protein folds with distinct interaction sites.
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V.Sureshan,
C.N.Deshpande,
Y.Boucher,
J.E.Koenig,
H.W.Stokes,
S.J.Harrop,
P.M.Curmi,
B.C.Mabbutt.
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ABSTRACT
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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.
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');
}
}
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