Journal:Acta Cryst F:S2053230X19002863
From Proteopedia
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<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. | <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. | ||
| - | <scene name='80/809196/Cv/11'>Ligand binding site</scene>. The L-Ala-SA molecule and residues involved in interactions with the ligand are shown as cyan and pink ball-and-sticks, respectively. Red balls represent the positions of water molecules. White dashed lines indicate hydrogen bonding. | + | <scene name='80/809196/Cv/11'>Ligand binding site</scene>. The L-Ala-SA molecule and residues involved in interactions with the ligand are shown as cyan and pink ball-and-sticks, respectively. Red balls represent the positions of water molecules. White dashed lines indicate hydrogen bonding. The adenine moiety is buried in a hydrophobic pocket that is lined by <scene name='80/809196/Cv/12'>Tyr310, Tyr411 and Ile340 on one side, and a loop (residues Gly286–Ala288)</scene> on the other side. This architecture stabilizes the purine base by hydrophobic and van der Waals interactions. Additionally, the <scene name='80/809196/Cv/13'>N6 amino group of the adenine ring interacts with the main chain carbonyl of Leu309 and the side-chain amide group of Asn308</scene>. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 13:11, 5 March 2019
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
