NMR Structure of the Heme Chaperone CcmE Reveals a Novel Functional Motif
نویسندگان
چکیده
منابع مشابه
Biochemical and mutational characterization of the heme chaperone CcmE reveals a heme binding site.
CcmE is a heme chaperone that binds heme transiently in the periplasm of Escherichia coli and delivers it to newly synthesized and exported c-type cytochromes. The chemical nature of the covalent bond between heme and H130 is not known. We have purified soluble histidine-tagged CcmE and present its spectroscopic characteristics in the visible range. Alanine scanning mutagenesis of conserved ami...
متن کاملDynamic ligation properties of the Escherichia coli heme chaperone CcmE to non-covalently bound heme.
The cytochrome c maturation protein CcmE is an essential membrane-anchored heme chaperone involved in the post-translational covalent attachment of heme to c-type cytochromes in Gram-negative bacteria such as Escherichia coli. Previous in vitro studies have shown that CcmE can bind heme both covalently (via a histidine residue) and non-covalently. In this work we present results on the latter f...
متن کاملPhysical interaction of CcmC with heme and the heme chaperone CcmE during cytochrome c maturation.
Biogenesis of c-type cytochromes requires the covalent attachment of heme to the apoprotein. In Escherichia coli, this process involves eight membrane proteins encoded by the ccmABCDEFGH operon. CcmE binds heme covalently and transfers it to apocytochromes c in the presence of other Ccm proteins. CcmC is necessary and sufficient to incorporate heme into CcmE. Here, we report that the CcmC prote...
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15 صفحه اولStructure of Hsp15 reveals a novel RNA-binding motif.
We have solved the crystal structure of the heat shock protein Hsp15, a newly isolated and very highly inducible heat shock protein that binds the ribosome. Comparison of its structure with those of two RNA-binding proteins, ribosomal protein S4 and threonyl-tRNA synthetase, reveals a novel RNA-binding motif. This newly recognized motif is remarkably common, present in at least eight different ...
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ژورنال
عنوان ژورنال: Structure
سال: 2002
ISSN: 0969-2126
DOI: 10.1016/s0969-2126(02)00885-7