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6HTV

Crystal structure of Leuconostoc citreum NRRL B-1299 N-terminally truncated dextransucrase DSR-M in complex with isomaltotetraose

Summary for 6HTV
Entry DOI10.2210/pdb6htv/pdb
DescriptorAlternansucrase, 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 Keywordsdextransucrase, dextran, transferase
Biological sourceLeuconostoc citreum
Total number of polymer chains1
Total formula weight144683.13
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 citationClaverie, 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: 31140266
DOI: 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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数据于2024-10-30公开中

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