3fs9 | pdb_00003fs9

Pseudomonas aeruginosa Azurin with mutated metal-binding loop sequence (CAAHAAM)

spinqualitylabelsall models 3fs9, resolution 1.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fs9 is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.05Å Ligands: CU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase. 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 The C-terminal copper-binding loop in the beta-barrel fold of the cupredoxin azurin has been replaced with a range of sequences containing alanine, glycine, and valine residues to assess the importance of amino acid composition and the length of this region. The introduction of 2 and 4 alanines between the coordinating Cys, His, and Met results in loop structures matching those in naturally occurring proteins with the same loop lengths. A loop with 4 alanines between the Cys and His and 3 between the His and Met ligands has a structure identical to that of the WT protein, whose loop is the same length. Loop structure is dictated by length and not sequence allowing the properties of the main surface patch for interactions with partners, to which the loop is a major contributor, to be optimized. Loops with 2 amino acids between the ligands using glycine, alanine, and valine residues have been compared. An empirical relationship is found between copper site protection by the loop and reduction potential. A loop adorned with 4 methyl groups is sufficient to protect the copper ion, enabling most sequences to adequately perform this task. The mutant with 3 alanine residues between the ligands forms a strand-swapped dimer in the crystal structure, an arrangement that has not, to our knowledge, been seen previously for this family of proteins. Cupredoxins function as redox shuttles and are required to be monomeric; therefore, none have evolved with a metal-binding loop of this length. Metal-binding loop length and not sequence dictates structure.,Sato K, Li C, Salard I, Thompson AJ, Banfield MJ, Dennison C Proc Natl Acad Sci U S A. 2009 Apr 7;106(14):5616-21. Epub 2009 Mar 19. PMID:19299503 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Azurin 3D structures

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