6g7n | pdb_00006g7n

Trichodesmium Tery_3377 (IdiA) (FutA) with iron and alanine ligand.

spinqualitylabelsall models 6g7n, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6g7n is a 2 chain structure with sequence from Trichodesmium erythraeum IMS101. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.1Å Ligands: DAL, DGL, FE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q10Z45_TRIEI Publication Abstract from PubMed Atmospheric nitrogen fixation by photosynthetic cyanobacteria (diazotrophs) strongly influences oceanic primary production and in turn affects global biogeochemical cycles. Species of the genus Trichodesmium are major contributors to marine diazotrophy, accounting for a significant proportion of the fixed nitrogen in tropical and subtropical oceans. However, Trichodesmium spp. are metabolically constrained by the availability of iron, an essential element for both the photosynthetic apparatus and the nitrogenase enzyme. Survival strategies in low-iron environments are typically poorly characterized at the molecular level, as these bacteria are recalcitrant to genetic manipulation. Here, we studied a homolog of the iron deficiency-induced A (IdiA)/ferric uptake transporter A (FutA) protein, Tery_3377, which has been used as an in situ iron-stress biomarker. IdiA/FutA has an ambiguous function in cyanobacteria, with its homologs hypothesized to be involved in distinct processes depending on their cellular localization. Using signal sequence fusions to GFP and heterologous expression in the model cyanobacterium Synechocystis sp. PCC 6803 we show that Tery_3377 is targeted to the periplasm by the twin-arginine translocase and can complement the deletion of the native Synechocystis ferric-iron ABC transporter periplasmic binding protein (FutA2). EPR spectroscopy revealed that purified recombinant Tery_3377 has specificity for iron in the Fe(3+) state, and an X-ray crystallography determined structure uncovered a functional iron substrate-binding domain, with Fe(3+) penta-coordinated by protein and buffer ligands. Our results support assignment of Tery_3377 as a functional FutA subunit of an Fe(3+) ABC-transporter, but do not rule out that it also has dual IdiA function. Structural and functional characterisation of IdiA/FutA (Tery_3377), an iron binding protein from the ocean diazotroph Trichodesmium erythraeum.,Polyviou D, Machelett MM, Hitchcock A, Baylay AJ, MacMillan F, Moore CM, Bibby TS, Tews I J Biol Chem. 2018 Sep 14. pii: RA118.001929. doi: 10.1074/jbc.RA118.001929. PMID:30217820 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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