Journal:Acta Cryst F:S2053230X19002863
From Proteopedia
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This paper describes the biochemical and structural analyses of adenylation enzyme IdnL7 involved in the biosynthesis of macrolactam antibiotic incednine. IdnL7 shows a broad substrate specificity for several small L-amino acids such as L-alanine and glycine. To obtain mechanistic insights into the substrate recognition of IdnL7, we determined the crystal structure of IdnL7 in complex with a reaction intermediate analog. IdnL7 has Cys217, Ala285 and Thr318 at the substrate binding pocket. These residues likely enable to accommodate various small L-amino acids as a substrate. This structural observation expands our understanding of the structure-function relationships of adenylation enzymes. | This paper describes the biochemical and structural analyses of adenylation enzyme IdnL7 involved in the biosynthesis of macrolactam antibiotic incednine. IdnL7 shows a broad substrate specificity for several small L-amino acids such as L-alanine and glycine. To obtain mechanistic insights into the substrate recognition of IdnL7, we determined the crystal structure of IdnL7 in complex with a reaction intermediate analog. IdnL7 has Cys217, Ala285 and Thr318 at the substrate binding pocket. These residues likely enable to accommodate various small L-amino acids as a substrate. This structural observation expands our understanding of the structure-function relationships of adenylation enzymes. | ||
| - | <scene name='80/809196/Cv/2'>Cartoon representation of the overall structure of IdnL7</scene>. The overall structure | + | <scene name='80/809196/Cv/2'>Cartoon representation of the overall structure of IdnL7</scene>. The overall structure of IdnL7 consists of two domains: a large <scene name='80/809196/Cv/3'>N-terminal domain</scene> (Met1–Gly413; in pink) and a smaller <scene name='80/809196/Cv/4'>C-terminal domain</scene> (Gln420–Leu522; in magenta). Both domains are connected by a <scene name='80/809196/Cv/5'>flexible hinge region</scene> (Arg414–Leu419), which allows for the rotation of the C-terminal domain during the two catalytic reaction steps. The N-terminal domain forms a <scene name='80/809196/Cv/6'>five-layered αβαβα-sandwich fold</scene>, whereas the C-terminal domain comprises <scene name='80/809196/Cv/7'>three helices with one two-stranded and one three-stranded antiparallel β-sheet</scene>. The C-terminal domain is arranged in the adenylation conformation in relation to the N-terminal domain. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 12:06, 5 March 2019
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