6HTV
Crystal structure of Leuconostoc citreum NRRL B-1299 N-terminally truncated dextransucrase DSR-M in complex with isomaltotetraose
6HTV の概要
| エントリーDOI | 10.2210/pdb6htv/pdb |
| 分子名称 | Alternansucrase, alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose, CALCIUM ION (3 entities in total) |
| 機能のキーワード | dextransucrase, dextran, transferase |
| 由来する生物種 | Leuconostoc citreum |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 144683.13 |
| 構造登録者 | Claverie, M.,Cioci, G.,Remaud-Simeon, M.,Moulis, C.,Lippens, G. (登録日: 2018-10-04, 公開日: 2019-09-11, 最終更新日: 2024-01-24) |
| 主引用文献 | Claverie, M.,Cioci, G.,Guionnet, M.,Schorghuber, J.,Lichtenecker, R.,Moulis, C.,Remaud-Simeon, M.,Lippens, G. Futile Encounter Engineering of the DSR-M Dextransucrase Modifies the Resulting Polymer Length. Biochemistry, 58:2853-2859, 2019 Cited by PubMed Abstract: The factors that define the resulting polymer length of distributive polymerases are poorly understood. Here, starting from the crystal structure of the dextransucrase DSR-M in complex with an isomaltotetraose, we define different anchoring points for the incoming acceptor. Mutation of one of these, Trp624, decreases the catalytic rate of the enzyme but equally skews the size distribution of the resulting dextran chains toward shorter chains. Nuclear magnetic resonance analysis shows that this mutation influences both the dynamics of the active site and the water accessibility. Monte Carlo simulation of the elongation process allows interpretation of these results in terms of enhanced futile encounters, whereby the less effective binding increases the pool of effective seeds for the dextran chains and thereby directly determines the length distribution of the final polymers. PubMed: 31140266DOI: 10.1021/acs.biochem.9b00373 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.9 Å) |
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