The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family
| Autor: | Nina Hakulinen, Mohammad Mubinur Rahman, Anu Koivula, Juha Rouvinen, Martina Andberg |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Protein family Stereochemistry Amino Acid Motifs 030106 microbiology lcsh:Medicine Crystallography X-Ray Article Substrate Specificity 03 medical and health sciences Tetramer Catalytic Domain Caulobacter crescentus Magnesium Amino Acid Sequence Binding site Protein Structure Quaternary lcsh:Science Hydro-Lyases X-ray crystallography Binding Sites Multidisciplinary biology Chemistry lcsh:R Active site Lyase biology.organism_classification Enzymes 030104 developmental biology Dehydratase Biocatalysis biology.protein lcsh:Q Protein quaternary structure Sequence Alignment |
| Zdroj: | Rahman, M M, Andberg, M, Koivula, A, Rouvinen, J & Hakulinen, N 2018, ' The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family ', Scientific Reports, vol. 8, no. 1, 865, pp. 865 . https://doi.org/10.1038/s41598-018-19192-6 Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018) Scientific Reports |
| DOI: | 10.1038/s41598-018-19192-6 |
| Popis: | The Ilv/ED dehydratase protein family includes dihydroxy acid-, gluconate-, 6-phosphogluconate- and pentonate dehydratases. The members of this family are involved in various biosynthetic and carbohydrate metabolic pathways. Here, we describe the first crystal structure of D-xylonate dehydratase from Caulobacter crescentus (CcXyDHT) at 2.7 Å resolution and compare it with other available enzyme structures from the IlvD/EDD protein family. The quaternary structure of CcXyDHT is a tetramer, and each monomer is composed of two domains in which the N-terminal domain forms a binding site for a [2Fe-2S] cluster and a Mg2+ ion. The active site is located at the monomer-monomer interface and contains residues from both the N-terminal recognition helix and the C-terminus of the dimeric counterpart. The active site also contains a conserved Ser490, which probably acts as a base in catalysis. Importantly, the cysteines that participate in the binding and formation of the [2Fe-2S] cluster are not all conserved within the Ilv/ED dehydratase family, which suggests that some members of the IlvD/EDD family may bind different types of [Fe-S] clusters. |
| Databáze: | OpenAIRE |
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