Journal:Acta Cryst F:S2053230X21008761
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| - | ) | + | <StructureSection load='' size='450' side='right' scene='89/890854/Cv/1' caption=''> |
| + | ===Complex structure of acyltransferase VinK and carrier protein VinL with a pantetheine cross-linking probe=== | ||
| + | <big>Akimasa Miyanaga, Risako Ouchi, Fumitaka Kudo and Tadashi Eguchi</big> <ref>doi: 10.1107/S2053230X21008761</ref> | ||
| + | <hr/> | ||
| + | <b>Molecular Tour</b><br> | ||
| + | Acyltransferases are responsible for the selective incorporation of an appropriate acyl building block in the biosynthesis of polyketide natural products. Proper protein-protein interactions between acyltransferase and cognate carrier protein are critical for the functional transfer of acyl groups. However, structural information on acyltransferase-carrier protein interactions is limited because of transient interactions between them. Understanding how each acyltransferase recognizes its cognate carrier protein is important for engineering polyketide biosynthetic pathways to produce novel compounds for drug discovery. | ||
| + | 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> (PDB entry [[7f2r]]). 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>. | ||
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| + | <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. | ||
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| + | '''PDB reference:''' VinK–VinL covalent complex with a pantetheineamide cross-linking probe, [[7f2r]]. | ||
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| + | <b>References</b><br> | ||
| + | <references/> | ||
| + | </StructureSection> | ||
| + | __NOEDITSECTION__ | ||
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