2nwv

Crystal structure of XisI protein-like (YP_323822.1) from Anabaena Variabilis ATCC 29413 at 1.85 A resolution

spinqualitylabelsall models 2nwv, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2nwv is a 1 chain structure with sequence from Trichormus variabilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function Q3M7V9_TRIV2 Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Nitrogen fixation is an important process that converts atmospheric gaseous nitrogen, a form plants cannot utilize, into ammonia that can be easily assimilated. Large serine recombinase XisF (fdxN element site-specific recombinase), together with controlling factors XisH and XisI, plays a critical role in the expression of nitrogen fixation genes of certain Anabaena and Nostoc species of cyanobacteria. All three proteins are required to excise the fdxN DNA element from the chromosome in differentiating heterocysts for the expression of nitrogen fixation related genes. We report the first crystal structures of XisH and XisI proteins, both adopting novel protein folds. Based on the analysis of their sequences and structures, we propose that XisH and XisI proteins function as endonucleases and recombination directionality factors (RDFs), respectively. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc. Site-specific recombination of nitrogen-fixation genes in cyanobacteria by XisF-XisH-XisI complex: Structures and models.,Hwang WC, Golden JW, Pascual J, Xu D, Cheltsov A, Godzik A Proteins. 2014 Sep 1. doi: 10.1002/prot.24679. PMID:25179344 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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