5VT4
Sco GlgEI-V279S in complex with a pyrolidene-based methyl-phosphonate compound
Summary for 5VT4
| Entry DOI | 10.2210/pdb5vt4/pdb |
| Related | 5VSJ |
| Descriptor | Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1, {[(2R,3R,4R,5R)-3-(alpha-D-glucopyranosyloxy)-4-hydroxy-2,5-bis(hydroxymethyl)pyrrolidin-1-yl]methyl}phosphonic acid (3 entities in total) |
| Functional Keywords | streptomyces coelicolor, maltosyltransferase, transition state analogue, alpha-1, 4-glucan, transferase |
| Biological source | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Total number of polymer chains | 4 |
| Total formula weight | 298393.81 |
| Authors | Petit, C.,Ronning, D.R.,Lindenberger, J.J. (deposition date: 2017-05-15, release date: 2017-06-07, Last modification date: 2023-10-04) |
| Primary citation | Veleti, S.K.,Petit, C.,Ronning, D.R.,Sucheck, S.J. Zwitterionic pyrrolidene-phosphonates: inhibitors of the glycoside hydrolase-like phosphorylase Streptomyces coelicolor GlgEI-V279S. Org. Biomol. Chem., 15:3884-3891, 2017 Cited by PubMed Abstract: We synthesized and evaluated new zwitterionic inhibitors against glycoside hydrolase-like phosphorylase Streptomyces coelicolor (Sco) GlgEI-V279S which plays a role in α-glucan biosynthesis. Sco GlgEI-V279S serves as a model enzyme for validated anti-tuberculosis (TB) target Mycobacterium tuberculosis (Mtb) GlgE. Pyrrolidine inhibitors 5 and 6 were designed based on transition state considerations and incorporate a phosphonate on the pyrrolidine moiety to expand the interaction network between the inhibitor and the enzyme active site. Compounds 5 and 6 inhibited Sco GlgEI-V279S with K = 45 ± 4 μM and 95 ± 16 μM, respectively, and crystal structures of Sco GlgE-V279S-5 and Sco GlgE-V279S-6 were obtained at a 3.2 Å and 2.5 Å resolution, respectively. PubMed: 28422240DOI: 10.1039/c7ob00388a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.205 Å) |
Structure validation
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