1s24

From Proteopedia

---

Revision as of 23:55, 20 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1s24 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Rubredoxin domain II from Pseudomonas oleovorans

Overview

Here we provide insights into the molecular structure of the two-iron, 19-kDa rubredoxin (AlkG) of Pseudomonas oleovorans using solution-state, nuclear magnetic resonance (NMR) and small-angle X-ray scattering studies., Sequence alignment and biochemical studies have suggested that AlkG, comprises two rubredoxin folds connected by a linker region of, approximately 70 amino acid residues. The C-terminal domain (C-Rb) of this, unusual rubredoxin, together with approximately 35 amino acid residues of, the predicted linker region, was expressed in Escherichia coli, purified, in the one-iron form and the structure of the cadmium-substituted form, determined at high-resolution by NMR spectroscopy. The structure shows, that the C-Rb domain is similar in fold to the conventional one-iron, rubredoxins from other organisms, whereas the linker region does not have, any discernible structure. This tandem "flexible-folded" structure of the, polypeptide chain derived for the C-Rb protein was confirmed using, solution X-ray scattering methods. X-ray scattering studies of AlkG, indicated that the 70-amino acid residue linker forms a structured, yet, mobile, polypeptide segment connecting the globular N- and C-terminal, domains. The X-ray scattering studies also showed that the N-terminal, domain (N-Rb) has a molecular conformation similar to that of C-Rb. The, restored molecular shape indicates that the folded N-Rb and C-Rb domains, of AlkG are noticeably separated, suggesting some domain movement on, complex formation with rubredoxin reductase to allow interdomain electron, transfer between the metal centers in AlkG. This study demonstrates the, advantage of combining X-ray scattering and NMR methods in structural, studies of dynamic, multidomain proteins that are not suited to, crystallographic analysis. The study forms a structural foundation for, functional studies of the interaction and electron-transfer reactions of, AlkG with rubredoxin reductase, also reported herein.

About this Structure

1S24 is a Single protein structure of sequence from Pseudomonas oleovorans with CD as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by NMR spectroscopy and solution X-ray scattering and interactions with rubredoxin reductase., Perry A, Tambyrajah W, Grossmann JG, Lian LY, Scrutton NS, Biochemistry. 2004 Mar 23;43(11):3167-82. PMID:15023067

Page seeded by OCA on Wed Nov 21 02:02:53 2007