2pya | pdb_00002pya

Ultra-high resolution structure of P. abyssi rubredoxin W4L/R5S/A44S

spinqualitylabelsall models 2pya, resolution 0.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pya is a 1 chain structure with sequence from "pyrococcus_abyssi"_erauso_et_al._1993 "pyrococcus abyssi" erauso et al. 1993. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, NA Related: 1yk5, 1yk4 Gene: rub ("Pyrococcus abyssi" Erauso et al. 1993) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RUBR_PYRAB] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule (By similarity). 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 effect of D-H...S(gamma)-Fe hydrogen bonding on the reduction potential of rubredoxin was investigated by the introduction of an O-H...S(gamma)-Fe hydrogen bond on the surface of Pyrococcus abyssi rubredoxin. The formation of a weak hydrogen bond between Ser44-O(gamma) and Cys42-S(gamma) in mutant W4L/R5S/A44S increased the reduction potential by 56 mV. When side effects of the mutation were taken into account, the contribution of the additional cluster hydrogen bond to the reduction potential was estimated to be +65 mV. The structural analysis was based on ultrahigh-resolution structures of oxidized P. abyssi rubredoxin W4L/R5S and W4L/R5S/A44S refined to 0.69 and 0.86 A, respectively. Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin: II. Introduction of an O-H...Sgamma-Fe hydrogen bond increased the reduction potential by 65 mV.,Bonisch H, Schmidt CL, Bianco P, Ladenstein R J Biol Inorg Chem. 2007 Nov;12(8):1163-71. Epub 2007 Aug 22. PMID:17712580 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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