This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2pya
From Proteopedia
Ultra-high resolution structure of P. abyssi rubredoxin W4L/R5S/A44S
Overview
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.
About this Structure
2PYA is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Wed Apr 30 13:16:33 2008
