1hlq
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(New page: 200px<br /><applet load="1hlq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hlq, resolution 1.45Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:31, 20 November 2007
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CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A
Overview
The crystal structure of Rhodoferax fermentans high-potential iron protein, (HiPIP) has been solved by MAD methods using the anomalous signal from the, Fe atoms in the [Fe(4)S(4)] cluster present in the protein and refined to, a resolution of 1.45 A. The peptide chain is well defined except in the N-, and C-terminal areas. The structure of the protein reveals the presence of, three helical fragments, a small beta-sheet and several turns, with the, [Fe(4)S(4)] cluster being located close to a surface patch containing, several well conserved aromatic residues. The protein fold is very similar, to the structures of other known HiPIPs, especially in the region proximal, to the [Fe(4)S(4)] cluster, while the largest differences are observed on, the opposite side of the protein, which is rich in positive charges and, has no sequential homology to other HiPIP families.
About this Structure
1HLQ is a Single protein structure of sequence from Rhodoferax fermentans with SO4 and SF4 as ligands. Full crystallographic information is available from OCA.
Reference
Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD., Gonzalez A, Benini S, Ciurli S, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1582-8. Epub 2003, Aug 19. PMID:12925788
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