Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases
. [Display omitted] ► Structural features of 2OG oxygenases involved in substrate recognition are analyzed. ► Crystallographic studies reveal the versatility of the jelly roll fold in substrate binding. ► Defined structural regions that interact with substrate(s) are biased by fold topology. ► The u...
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Published in | Current opinion in structural biology Vol. 22; no. 6; pp. 691 - 700 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
01.12.2012
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Subjects | |
Online Access | Get full text |
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Summary: | . [Display omitted]
► Structural features of 2OG oxygenases involved in substrate recognition are analyzed. ► Crystallographic studies reveal the versatility of the jelly roll fold in substrate binding. ► Defined structural regions that interact with substrate(s) are biased by fold topology. ► The utility of the enzyme–substrate structures for engineering and selective inhibition are discussed.
2-Oxoglutarate (2OG) and ferrous iron dependent oxygenases catalyze two-electron oxidations of a range of small and large molecule substrates, including proteins/peptides/amino acids, nucleic acids/bases, and lipids, as well as natural products including antibiotics and signaling molecules. 2OG oxygenases employ variations of a core double-stranded β-helix (DSBH; a.k.a. jelly-roll, cupin or jumonji C (JmjC)) fold to enable binding of Fe(II) and 2OG in a subfamily conserved manner. The topology of the DSBH limits regions directly involved in substrate binding: commonly the first, second and eighth strands, loops between the second/third and fourth/fifth DSBH strands, and the N-terminal and C-terminal regions are involved in primary substrate, co-substrate and cofactor binding. Insights into substrate recognition by 2OG oxygenases will help to enable selective inhibition and bioengineering studies. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0959-440X 1879-033X |
DOI: | 10.1016/j.sbi.2012.10.001 |