PMID:10550687

Citation	Duhme, AK, Meyer-Klaucke, W, White, DJ, Delarbre, L, Mitchenall, LA and Pau, RN (1999) Extended X-ray absorption fine structure studies on periplasmic and intracellular molybdenum-binding proteins. J. Biol. Inorg. Chem. 4:588-92
Abstract	We have studied the molybdenum K-edge X-ray absorption spectra of Mo bound in the Mo-binding proteins Mop from Haemophilus influenzae, ModG from Azotobacter vinelandii and the Escherichia coli ModE transcriptional regulatory protein, and compared them with the absorption spectra of A. vinelandii ModA and monomeric molybdate. Pre-edge and extended fine structure data indicate that the Mo-binding proteins with molbindin-like domains bind tetrahedral molybdate with a Mo-O distance of 1.76 A. The molbindin subunits or sub-domains represent a novel protein fold that is used by proteins with distinct functions to bind molybdate in the cytoplasm. The high specificity of the proteins for molybdenum does not depend on a change of coordination number or geometry.
Links	PubMed
Keywords	Azotobacter vinelandii/chemistry; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Carrier Proteins/chemistry; Escherichia coli/chemistry; Haemophilus influenzae/chemistry; Molybdenum/chemistry; Molybdenum/metabolism; Protein Structure, Secondary; Spectrum Analysis
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.