3tbn | pdb_00003tbn

Crystal structure of a miner2 homolog: a type 6 CDGSH iron-sulfur protein.

spinqualitylabelsall models 3tbn, resolution 1.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tbn is a 1 chain structure with sequence from Magnetospirillum magneticum AMB-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.15Å Ligands: FES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2W014_PARM1 Publication Abstract from PubMed The recently discovered CDGSH iron-sulfur domains (CISDs) are classified into seven major types with a wide distribution throughout the three domains of life. The type 1 protein mitoNEET has been shown to fold into a dimer with the signature CDGSH motif binding to a [2Fe-2S] cluster. However, the structures of all other types of CISDs were unknown. Here we report the crystal structures of type 3, 4, and 6 CISDs determined at 1.5 A, 1.8 A and 1.15 A resolution, respectively. The type 3 and 4 CISD each contain one CDGSH motif and adopt a dimeric structure. Although similar to each other, the two structures have permutated topologies, and both are distinct from the type 1 structure. The type 6 CISD contains tandem CDGSH motifs and adopts a monomeric structure with an internal pseudo dyad symmetry. All currently known CISD structures share dual iron-sulfur binding modules and a beta-sandwich for either intermolecular or intramolecular dimerization. The iron-sulfur binding module, the beta-strand N-terminal to the module and a proline motif are conserved among different type structures, but the dimerization module and the interface and orientation between the two iron-sulfur binding modules are divergent. Sequence analysis further shows resemblance between CISD types 4 and 7 and between 1 and 2. Our findings suggest that all CISDs share common ancestry and diverged into three primary folds with a characteristic phylogenetic distribution: a eukaryote-specific fold adopted by types 1 and 2 proteins, a prokaryote-specific fold adopted by types 3, 4 and 7 proteins, and a tandem-motif fold adopted by types 5 and 6 proteins. Our comprehensive structural, sequential and phylogenetic analysis provides significant insight into the assembly principles and evolutionary relationship of CISDs. Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains.,Lin J, Zhang L, Lai S, Ye K PLoS One. 2011;6(9):e24790. Epub 2011 Sep 16. PMID:21949752 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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