3TBO

Crystal structure of a type 3 CDGSH iron-sulfur protein.

Summary for 3TBO

• Entry DOI: 10.2210/pdb3tbo/pdb
• Related: 3TBM 3TBN
• Descriptor: Zinc finger, CDGSH-type domain protein, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• Functional Keywords: cdgsh, iron-sulfur, metal binding protein
• Biological source: Pyrobaculum calidifontis
• Total number of polymer chains: 1
• Total formula weight: 6748.41

Authors

Lin, J.,Zhang, L.,Ye, K. (deposition date: 2011-08-07, release date: 2011-10-05, Last modification date: 2024-03-20)

Primary citation

Lin, J.,Zhang, L.,Lai, S.,Ye, K.
Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains.
Plos One, 6:e24790-e24790, 2011

PubMed Abstract: 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 Å, 1.8 Å and 1.15 Å 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 β-sandwich for either intermolecular or intramolecular dimerization. The iron-sulfur binding module, the β-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.

PubMed: 21949752
DOI: 10.1371/journal.pone.0024790

Experimental method

X-RAY DIFFRACTION (1.5 Å)