Structural highlights
Function
[HIP_ALLVD] Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria.
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 crystal structure of Chromatium vinosum C77S HiPIP has been determined and is compared with that of wild type. This is the first reported crystal structure of a Ser ligated [4Fe-4S] cluster and reveals a 0.11 A shortening of the Fe-O bond (relative to Fe-S), but only minor structural alterations of the overall tertiary structure. Coordination changes are corroborated by resonance Raman spectroscopy. Comparison of the crystal and solution structures for HiPIPs identifies Phe48 as the main controller of solvent access to the Fe-S cluster; however, there is no significant change in cluster solvation of the C77S mutant relative to WT HiPIP. Ser ligation ultimately results in decreased cluster stability due to increased sensitivity to proton mediated degradation.
Crystal structure and stability studies of C77S HiPIP: a serine ligated [4Fe-4S] cluster.,Mansy SS, Xiong Y, Hemann C, Hille R, Sundaralingam M, Cowan JA Biochemistry. 2002 Jan 29;41(4):1195-201. PMID:11802718[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mansy SS, Xiong Y, Hemann C, Hille R, Sundaralingam M, Cowan JA. Crystal structure and stability studies of C77S HiPIP: a serine ligated [4Fe-4S] cluster. Biochemistry. 2002 Jan 29;41(4):1195-201. PMID:11802718
