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Structure of the E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) from Thermus thermophilus.
- Source :
-
FEBS letters [FEBS Lett] 2011 Feb 04; Vol. 585 (3), pp. 447-51. Date of Electronic Publication: 2010 Dec 15. - Publication Year :
- 2011
-
Abstract
- Isoprenoids are biosynthesized via the mevalonate or the 2-C-methyl-d-erythritol-4-phosphate (MEP) pathways the latter being used by most pathogenic bacteria, some parasitic protozoa, plant plastids, but not by animals. We determined the X-ray structure of the homodimeric [4Fe-4S] cluster carrying E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) of Thermus thermophilus which catalyzes the penultimate reaction of the MEP pathway and is therefore an attractive target for drug development. The [4Fe-4S] cluster ligated to three cysteines and one glutamate is encapsulated at the intersubunit interface. The substrate binding site lies in front of an (αβ)(8) barrel. The great [4Fe-4S] cluster-substrate distance implicates large-scale domain rearrangements during the reaction cycle.<br /> (Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Bacterial Proteins genetics
Bacterial Proteins metabolism
Biocatalysis
Catalytic Domain
Crystallography, X-Ray
Enzymes genetics
Enzymes metabolism
Iron-Sulfur Proteins chemistry
Iron-Sulfur Proteins genetics
Iron-Sulfur Proteins metabolism
Protein Conformation
Protein Interaction Domains and Motifs
Protein Multimerization
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Bacterial Proteins chemistry
Enzymes chemistry
Thermus thermophilus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 585
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 21167158
- Full Text :
- https://doi.org/10.1016/j.febslet.2010.12.012