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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
Function and structure of the molybdenum cofactor carrier protein from Chlamydomonas reinhardtii
Journal of Biological Chemistry, Volume 281, No. 40, Year 2006
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Description
The molybdenum cofactor (Moco) forms the catalytic site in all eukaryotic molybdenum enzymes and is synthesized by a multistep biosynthetic pathway. The mechanism of transfer, storage, and insertion of Moco into the appropriate apo-enzyme is poorly understood. In Chlamydomonas reinhardtii, a Moco carrier protein (MCP) has been identified and characterized recently. Here we show biochemical evidence that MCP binds Moco as well as the tungstate-substituted form of the cofactor (Wco) with high affinity, whereas molybdopterin, the ultimate cofactor precursor, is not bound. This binding selectivity points to a specific metal-mediated interaction with MCP, which protects Moco and Wco from oxidation with t1/2 of 24 and 96 h, respectively. UV-visible spectroscopy showed defined absorption bands at 393, 470, and 570 nm pointing to ene-diothiolate and protein side-chain charge transfer bonds with molybdenum. We have determined the crystal structure of MCP at 1.6 Å resolution using seleno-methionated and native protein. The monomer constitutes a Rossmann fold with two homodimers forming a symmetrical tetramer in solution. Based on conserved surface residues, charge distribution, shape, in silico docking studies, structural comparisons, and identification of an anion-binding site, a prominent surface depression was proposed as a Moco-binding site, which was confirmed by structure-guided mutagenesis coupled to substrate binding studies. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.
Authors & Co-Authors
Kuper, Jochen
Germany, Hamburg
European Molecular Biology Laboratory Hamburg
Ataya, Farid Shokry
Spain, Cordoba
Universidad de Córdoba
Mendel, Ralf Rainer
Germany, Braunschweig
Technische Universität Braunschweig
Statistics
Citations: 66
Authors: 3
Affiliations: 5
Identifiers
Doi:
10.1074/jbc.M603919200
ISSN:
1083351X
Research Areas
Mental Health