5I0D
Cycloalternan-forming enzyme from Listeria monocytogenes in complex with cycloalternan
Summary for 5I0D
| Entry DOI | 10.2210/pdb5i0d/pdb |
| Related | 4KWU 5F7U 5I0E 5I0F 5I0G |
| Descriptor | Lmo2446 protein, alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose, Cyclic alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose, ... (10 entities in total) |
| Functional Keywords | complex, structural genomics, center for structural genomics of infectious diseases, csgid, sugar binding protein |
| Biological source | Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) |
| Total number of polymer chains | 2 |
| Total formula weight | 246759.52 |
| Authors | Light, S.H.,Minasov, G.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2016-02-03, release date: 2016-12-14, Last modification date: 2024-10-30) |
| Primary citation | Light, S.H.,Cahoon, L.A.,Mahasenan, K.V.,Lee, M.,Boggess, B.,Halavaty, A.S.,Mobashery, S.,Freitag, N.E.,Anderson, W.F. Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity. Structure, 25:295-304, 2017 Cited by PubMed Abstract: Active in the aqueous cellular environment where a massive excess of water is perpetually present, enzymes that catalyze the transfer of an electrophile to a non-water nucleophile (transferases) require specific strategies to inhibit mechanistically related hydrolysis reactions. To identify principles that confer transferase versus hydrolase reaction specificity, we exploited two enzymes that use highly similar catalytic apparatuses to catalyze the transglycosylation (a transferase reaction) or hydrolysis of α-1,3-glucan linkages in the cyclic tetrasaccharide cycloalternan (CA). We show that substrate binding to non-catalytic domains and a conformationally stable active site promote CA transglycosylation, whereas a distinct pattern of active site conformational change is associated with CA hydrolysis. These findings defy the classic view of induced-fit conformational change and illustrate a mechanism by which a stable hydrophobic binding site can favor transferase activity and disfavor hydrolysis. Application of these principles could facilitate the rational reengineering of transferases with desired catalytic properties. PubMed: 28089449DOI: 10.1016/j.str.2016.12.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
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