4A34
Crystal structure of the fucose mutarotase in complex with L-fucose from Streptococcus pneumoniae
Summary for 4A34
| Entry DOI | 10.2210/pdb4a34/pdb |
| Descriptor | RBSD/FUCU TRANSPORT PROTEIN FAMILY PROTEIN, beta-L-fucopyranose, POTASSIUM ION, ... (4 entities in total) |
| Functional Keywords | isomerase |
| Biological source | STREPTOCOCCUS PNEUMONIAE |
| Total number of polymer chains | 20 |
| Total formula weight | 335155.98 |
| Authors | Higgins, M.A.,Boraston, A.B. (deposition date: 2011-09-29, release date: 2011-10-12, Last modification date: 2024-05-08) |
| Primary citation | Higgins, M.A.,Boraston, A.B. Structure of the Fucose Mutarotase from Streptococcus Pneumoniae in Complex with L-Fucose Acta Crystallogr.,Sect.F, 67:1524-, 2011 Cited by PubMed Abstract: Streptococcus pneumoniae relies on a variety of carbohydrate-utilization pathways for both colonization of its human host and full virulence during the development of invasive disease. One such pathway is the fucose-utilization pathway, a component of which is fucose mutarotase (SpFcsU), an enzyme that performs the interconversion between α-L-fucose and β-L-fucose. This protein was crystallized and its three-dimensional structure was solved in complex with L-fucose. The structure shows a complex decameric quaternary structure with a high overall degree of structural identity to Escherichia coli FcsU (EcFcsU). Furthermore, the active-site architecture of SpFcsU is highly similar to that of EcFcsU. When considered in the context of the fucose-utilization pathway found in S. pneumoniae, SpFcsU appears to link the two halves of the pathway by enhancing the rate of conversion of the product of the final glycoside hydrolysis step, β-fucose, into the substrate for the fucose isomerase, α-fucose. PubMed: 22139157DOI: 10.1107/S1744309111046343 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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