Experimental phasing with vanadium and application to nucleotide-binding membrane proteins (291 views)
Iucrj (ISSN: 2052-2525linking), 2020 Oct 14; 7(Pt6): 1092-1101.
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Paper type: Journal Article,
Impact factor: 5.4, 5-year impact factor: 5.562
Url: https://doi.org/10.1107/S2052252520012312
Keywords: Experimental Phasing, Vanadium, Membrane Proteins,
Affiliations:
*** IBB - CNR ***
Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, United Kingdom., Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot OX11 0FA, United Kingdom., Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom., Department of Life Sciences, Imperial College, London, United Kingdom., Institute of Biostructures and Bioimaging, National Research Council (IBB-CNR), Via Mezzocannone 16, 80134 Napoli, Italy., Department of Biomedicine, Aarhus University, Ole Worms Allé 8, DK-8000 Aarhus, Denmark.,
References:
Not available.
Iucrj (ISSN: 2052-2525linking), 2020 Oct 14; 7(Pt6): 1092-1101.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.4, 5-year impact factor: 5.562
Url: https://doi.org/10.1107/S2052252520012312
Keywords: Experimental Phasing, Vanadium, Membrane Proteins,
Affiliations:
*** IBB - CNR ***
Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, United Kingdom., Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot OX11 0FA, United Kingdom., Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom., Department of Life Sciences, Imperial College, London, United Kingdom., Institute of Biostructures and Bioimaging, National Research Council (IBB-CNR), Via Mezzocannone 16, 80134 Napoli, Italy., Department of Biomedicine, Aarhus University, Ole Worms Allé 8, DK-8000 Aarhus, Denmark.,
References:
Not available.
Experimental phasing with vanadium and application to nucleotide-binding membrane proteins
The structure determination of soluble and membrane proteins can be hindered by the crystallographic phase problem, especially in the absence of a suitable homologous structure. Experimental phasing is the method of choice for novel structures; however, it often requires heavy-atom derivatization, which can be difficult and time-consuming. Here, a novel and rapid method to obtain experimental phases for protein structure determination by vanadium phasing is reported. Vanadate is a transition-state mimic of phosphoryl-transfer reactions and it has the advantage of binding specifically to the active site of numerous enzymes catalyzing this reaction. The applicability of vanadium phasing has been validated by determining the structures of three different protein-vanadium complexes, two of which are integral membrane proteins: the rabbit sarcoplasmic reticulum Ca(2+)-ATPase, the antibacterial peptide ATP-binding cassette transporter McjD from Escherichia coli and the soluble enzyme RNAse A from Bos taurus. Vanadium phasing was successful even at low resolution and despite severe anisotropy in the data. This method is principally applicable to a large number of proteins, representing six of the seven Enzyme Commission classes. It relies exclusively on the specific chemistry of the protein and it does not require any modifications, making it a very powerful addition to the phasing toolkit. In addition to the phasing power of this technique, the protein-vanadium complexes also provide detailed insights into the reaction mechanisms of the studied proteins.
The structure determination of soluble and membrane proteins can be hindered by the crystallographic phase problem, especially in the absence of a suitable homologous structure. Experimental phasing is the method of choice for novel structures; however, it often requires heavy-atom derivatization, which can be difficult and time-consuming. Here, a novel and rapid method to obtain experimental phases for protein structure determination by vanadium phasing is reported. Vanadate is a transition-state mimic of phosphoryl-transfer reactions and it has the advantage of binding specifically to the active site of numerous enzymes catalyzing this reaction. The applicability of vanadium phasing has been validated by determining the structures of three different protein-vanadium complexes, two of which are integral membrane proteins: the rabbit sarcoplasmic reticulum Ca(2+)-ATPase, the antibacterial peptide ATP-binding cassette transporter McjD from Escherichia coli and the soluble enzyme RNAse A from Bos taurus. Vanadium phasing was successful even at low resolution and despite severe anisotropy in the data. This method is principally applicable to a large number of proteins, representing six of the seven Enzyme Commission classes. It relies exclusively on the specific chemistry of the protein and it does not require any modifications, making it a very powerful addition to the phasing toolkit. In addition to the phasing power of this technique, the protein-vanadium complexes also provide detailed insights into the reaction mechanisms of the studied proteins.
Experimental phasing with vanadium and application to nucleotide-binding membrane proteins
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Experimental phasing with vanadium and application to nucleotide-binding membrane proteins
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
16 Records (15 excluding Abstracts).
Total impact factor: 123.261 (113.918 excluding Abstracts).
Total 5 year impact factor: 117.354 (107.733 excluding Abstracts).
Total impact factor: 123.261 (113.918 excluding Abstracts).
Total 5 year impact factor: 117.354 (107.733 excluding Abstracts).
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