3LNP

Crystal Structure of Amidohydrolase family Protein OLEI01672_1_465 from Oleispira antarctica


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.184 
  • R-Value Work: 0.149 
  • R-Value Observed: 0.151 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Genome sequence and functional genomic analysis of the oil-degrading bacterium Oleispira antarctica.

Kube, M.Chernikova, T.N.Al-Ramahi, Y.Beloqui, A.Lopez-Cortez, N.Guazzaroni, M.E.Heipieper, H.J.Klages, S.Kotsyurbenko, O.R.Langer, I.Nechitaylo, T.Y.Lunsdorf, H.Fernandez, M.Juarez, S.Ciordia, S.Singer, A.Kagan, O.Egorova, O.Petit, P.A.Stogios, P.Kim, Y.Tchigvintsev, A.Flick, R.Denaro, R.Genovese, M.Albar, J.P.Reva, O.N.Martinez-Gomariz, M.Tran, H.Ferrer, M.Savchenko, A.Yakunin, A.F.Yakimov, M.M.Golyshina, O.V.Reinhardt, R.Golyshin, P.N.

(2013) Nat Commun 4: 2156-2156

  • DOI: https://doi.org/10.1038/ncomms3156
  • Primary Citation of Related Structures:  
    3I4Q, 3IRU, 3LMB, 3LNP, 3M16, 3QVM, 3V77, 3VCR

  • PubMed Abstract: 

    Ubiquitous bacteria from the genus Oleispira drive oil degradation in the largest environment on Earth, the cold and deep sea. Here we report the genome sequence of Oleispira antarctica and show that compared with Alcanivorax borkumensis--the paradigm of mesophilic hydrocarbonoclastic bacteria--O. antarctica has a larger genome that has witnessed massive gene-transfer events. We identify an array of alkane monooxygenases, osmoprotectants, siderophores and micronutrient-scavenging pathways. We also show that at low temperatures, the main protein-folding machine Cpn60 functions as a single heptameric barrel that uses larger proteins as substrates compared with the classical double-barrel structure observed at higher temperatures. With 11 protein crystal structures, we further report the largest set of structures from one psychrotolerant organism. The most common structural feature is an increased content of surface-exposed negatively charged residues compared to their mesophilic counterparts. Our findings are relevant in the context of microbial cold-adaptation mechanisms and the development of strategies for oil-spill mitigation in cold environments.


  • Organizational Affiliation

    Max-Planck Institute for Molecular Genetics, Berlin-Dahlem D-14195, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Amidohydrolase family Protein OLEI01672_1_465468Oleispira antarcticaMutation(s): 0 
UniProt
Find proteins for D3KFX9 (Oleispira antarctica)
Explore D3KFX9 
Go to UniProtKB:  D3KFX9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupD3KFX9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.184 
  • R-Value Work: 0.149 
  • R-Value Observed: 0.151 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 77.902α = 90
b = 77.902β = 90
c = 143.754γ = 120
Software Package:
Software NamePurpose
SBC-Collectdata collection
HKL-3000data collection
HKL-3000phasing
SHELXSphasing
MLPHAREphasing
RESOLVEmodel building
SOLVEphasing
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling
RESOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-02-16
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2013-12-25
    Changes: Database references