6HTV
Crystal structure of Leuconostoc citreum NRRL B-1299 N-terminally truncated dextransucrase DSR-M in complex with isomaltotetraose
Summary for 6HTV
Entry DOI | 10.2210/pdb6htv/pdb |
Descriptor | 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) |
Functional Keywords | dextransucrase, dextran, transferase |
Biological source | Leuconostoc citreum |
Total number of polymer chains | 1 |
Total formula weight | 144683.13 |
Authors | Claverie, M.,Cioci, G.,Remaud-Simeon, M.,Moulis, C.,Lippens, G. (deposition date: 2018-10-04, release date: 2019-09-11, Last modification date: 2024-01-24) |
Primary citation | 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 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.9 Å) |
Structure validation
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