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PDBsum entry 3fuy

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protein ligands Protein-protein interface(s) links
Structural genomics, unknown function PDB id
3fuy

 

 

 

 

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Contents
Protein chains
156 a.a.
Ligands
SO4
Waters ×163
PDB id:
3fuy
Name: Structural genomics, unknown function
Title: Structure from the mobile metagenome of cole harbour salt marsh: integron cassette protein hfx_cass1
Structure: Putative integron gene cassette protein. Chain: a, b, c. Synonym: hfx_cass1. Engineered: yes
Source: Uncultured bacterium. Organism_taxid: 77133. Gene: orf1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.199     R-free:   0.234
Authors: 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)
Key ref: V.Sureshan et al. (2013). Integron gene cassettes: a repository of novel protein folds with distinct interaction sites. Plos One, 8, e52934. PubMed id: 23349695
Date:
15-Jan-09     Release date:   24-Feb-09    
PROCHECK
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 Headers
 References

Protein chains
B0BGB0  (B0BGB0_9BACT) -  Putative integron gene cassette protein from uncultured bacterium
Seq:
Struc:
158 a.a.
156 a.a.
Key:    Secondary structure  CATH domain

 

 
Plos One 8:e52934 (2013)
PubMed id: 23349695  
 
 
Integron gene cassettes: a repository of novel protein folds with distinct interaction sites.
V.Sureshan, C.N.Deshpande, Y.Boucher, J.E.Koenig, H.W.Stokes, S.J.Harrop, P.M.Curmi, B.C.Mabbutt.
 
  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.
 

 

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