Structural highlights
Function
[PUFX_RHOS4] Associated with the reaction center - light-harvesting complex I. May play a critical role in facilitating the interaction between this complex and other components required for light-driven cyclic electron transfer.
Publication Abstract from PubMed
PufX organizes the photosynthetic reaction centre-light harvesting complex 1 (RC-LH1) core complex of Rhodobacter sphaeroides and facilitates quinol/quinone exchange between the RC and cytochrome bc(1) complexes. The structure of PufX in organic solvent reveals two hydrophobic helices flanked by unstructured termini and connected by a helical bend. The proposed location of basic residues and tryptophans at the membrane interface orients the C-terminal helix along the membrane normal, with the GXXXG motifs in positions unsuitable as direct drivers of dimerisation of the RC-LH1 complex. The N-terminal helix is predicted to extend approximately 40 Anggstrom along the membrane interface.
The solution structure of the PufX polypeptide from Rhodobacter sphaeroides.,Tunnicliffe RB, Ratcliffe EC, Hunter CN, Williamson MP FEBS Lett. 2006 Dec 22;580(30):6967-71. Epub 2006 Dec 4. PMID:17161397[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tunnicliffe RB, Ratcliffe EC, Hunter CN, Williamson MP. The solution structure of the PufX polypeptide from Rhodobacter sphaeroides. FEBS Lett. 2006 Dec 22;580(30):6967-71. Epub 2006 Dec 4. PMID:17161397 doi:http://dx.doi.org/S0014-5793(06)01406-2
