5fc9

Novel Purple Cupredoxin from Nitrosopumilus maritimus

spinqualitylabelsall models 5fc9, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fc9 is a 4 chain structure with sequence from Nitrosopumilus maritimus SCM1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: CU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A9A2G4_NITMS Publication Abstract from PubMed Mononuclear cupredoxin proteins usually contain a coordinately saturated type 1 copper (T1Cu) center and function exclusively as electron carriers. Here we report a cupredoxin isolated from the nitrifying archaeon Nitrosopumilus maritimus SCM1, called Nmar1307, that contains a T1Cu center with an open binding site containing water. It displays a deep purple color due to strong absorptions around 413 nm (1880 M-1 cm-1) and 558 nm (2290 M-1 cm-1) in the UV-vis electronic spectrum. EPR studies suggest the protein contains two Cu(II) species of nearly equal population, one nearly axial, with hyperfine constant A parallel = 98 x 10-4 cm-1, and another more rhombic, with a smaller A parallel value of 69 x 10-4 cm-1. The X-ray crystal structure at 1.6 A resolution confirms that it contains a Cu atom coordinated by two His and one Cys in a trigonal plane, with an axial H2O at 2.25 A. Both UV-vis absorption and EPR spectroscopic studies suggest that the Nmar1307 can oxidize NO to nitrite, an activity that is attributable to the high reduction potential (354 mV vs SHE) of the copper site. These results suggest that mononuclear cupredoxins can have a wide range of structural features, including an open binding site containing water, making this class of proteins even more versatile. A Purple Cupredoxin from Nitrosopumilus maritimus Containing a Mononuclear Type 1 Copper Center with an Open Binding Site.,Hosseinzadeh P, Tian S, Marshall NM, Hemp J, Mullen T, Nilges MJ, Gao YG, Robinson H, Stahl DA, Gennis RB, Lu Y J Am Chem Soc. 2016 May 12. PMID:27120678 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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