Journal:Acta Cryst F:S2053230X21008761
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The acyltransferase VinK specifically interacts with the carrier protein VinL for substrate transfer in the biosynthesis of macrolactam antibiotic vicenistatin. The crystal structure of the VinK-VinL covalent complex formed with 1,2-bismaleimidoethane cross-linker has been determined previously. This paper describes the structural determination of <scene name='89/890854/Cv/3'>the VinK-VinL complex formed with a pantetheine cross-linking probe</scene>. The α/β hydrolase (ABH) domain of VinK, ferredoxin-like (FL) domain of VinK and VinL are shown in green, yellow-green and cyan, respectively. Ser36 of VinL, the phosphopantetheine analog moiety derived from the pantetheine probe and Cys106 of the VinK S106C mutant are shown as stick representations. <scene name='89/890854/Cv/6'>Pantetheine binding region in the VinK-VinL complex formed with a pantetheine cross-linking probe</scene>. | The acyltransferase VinK specifically interacts with the carrier protein VinL for substrate transfer in the biosynthesis of macrolactam antibiotic vicenistatin. The crystal structure of the VinK-VinL covalent complex formed with 1,2-bismaleimidoethane cross-linker has been determined previously. This paper describes the structural determination of <scene name='89/890854/Cv/3'>the VinK-VinL complex formed with a pantetheine cross-linking probe</scene>. The α/β hydrolase (ABH) domain of VinK, ferredoxin-like (FL) domain of VinK and VinL are shown in green, yellow-green and cyan, respectively. Ser36 of VinL, the phosphopantetheine analog moiety derived from the pantetheine probe and Cys106 of the VinK S106C mutant are shown as stick representations. <scene name='89/890854/Cv/6'>Pantetheine binding region in the VinK-VinL complex formed with a pantetheine cross-linking probe</scene>. | ||
| - | <scene name='89/890854/Cv/9'>The interface interactions between VinK and VinL</scene> | + | <scene name='89/890854/Cv/9'>The interface interactions between VinK and VinL</scene> are essentially the same between these two VinK-VinL complex structures, suggesting that interface interactions are not affected by the cross-linking strategy used. This structural observation expands our understanding of the structure-function relationships of acyltransferases. Salt bridges are shown as dashed lines, helix II is colored in deep sky blue. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 14:26, 24 August 2021
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