5AXH
Crystal structure of thermophilic dextranase from Thermoanaerobacter pseudethanolicus, D312G mutant in complex with isomaltohexaose
Summary for 5AXH
| Entry DOI | 10.2210/pdb5axh/pdb |
| Related | 5AXG |
| Descriptor | Dextranase, alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-6)-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | glycoside hydrolase family 66, hydrolase |
| Biological source | Thermoanaerobacter pseudethanolicus ATCC 33223 |
| Total number of polymer chains | 2 |
| Total formula weight | 144876.48 |
| Authors | Suzuki, N.,Kishine, N.,Fujimoto, Z.,Sakurai, M.,Momma, M.,Ko, J.A.,Nam, S.H.,Kimura, A.,Kim, Y.M. (deposition date: 2015-07-29, release date: 2015-11-11, Last modification date: 2023-11-08) |
| Primary citation | Suzuki, N.,Kishine, N.,Fujimoto, Z.,Sakurai, M.,Momma, M.,Ko, J.A.,Nam, S.H.,Kimura, A.,Kim, Y.M. Crystal structure of thermophilic dextranase from Thermoanaerobacter pseudethanolicus J.Biochem., 159:331-339, 2016 Cited by PubMed Abstract: The crystal structures of the wild type and catalytic mutant Asp-312→Gly in complex with isomaltohexaose of endo-1,6-dextranase from the thermophilic bacterium Thermoanaerobacter pseudethanolicus (TpDex), belonging to the glycoside hydrolase family 66, were determined. TpDex consists of three structural domains, a catalytic domain comprising an (β/α)8-barrel and two β-domains located at both N- and C-terminal ends. The isomaltohexaose-complex structure demonstrated that the isomaltohexaose molecule was bound across the catalytic site, showing that TpDex had six subsites (-4 to +2) in the catalytic cleft. Marked movement of the Trp-376 side-chain along with loop 6, which was the side wall component of the cleft at subsite +1, was observed to occupy subsite +1, indicating that it might expel the cleaved aglycone subsite after the hydrolysis reaction. Structural comparison with other mesophilic enzymes indicated that several structural features of TpDex, loop deletion, salt bridge and surface-exposed charged residue, may contribute to thermostability. PubMed: 26494689DOI: 10.1093/jb/mvv104 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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