Literature DB >> 16511263

Purification, crystallization and preliminary X-ray analysis of the outer membrane complex HasA-HasR from Serratia marcescens.

Frédéric Huché1, Philippe Delepelaire, Cécile Wandersman, Wolfram Welte.   

Abstract

Serratia marcescens is able to acquire iron using its haem-acquisition system (;has'), which contains an outer membrane receptor HasR and a soluble haemophore HasA. After secretion, HasA binds free haem in the extracellular medium or extracts it from haemoproteins and delivers it to the receptor. Here, the crystallization of a HasA-HasR complex is reported. HasA and HasR have been overexpressed in Escherichia coli and the complex formed and crystallized. Small platelets and bunches of needles of dimensions 0.01 x 0.1 x 1 mm were obtained. A native data set has been collected to 6.8 A.

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Year:  2005        PMID： 16511263      PMCID： PMC2150924          DOI： 10.1107/S1744309105041394

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  23 in total

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Review 4.  Siderophores: structure and function of microbial iron transport compounds.

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5.  Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide.

Authors:  A D Ferguson; E Hofmann; J W Coulton; K Diederichs; W Welte
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6.  A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli.

Authors:  J M Ghigo; S Létoffé; C Wandersman
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  4 in total

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3.  Pyridine Hemochromagen Assay for Determining the Concentration of Heme in Purified Protein Solutions.

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  4 in total

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