5HOQ

Apo structure of CalS11, TDP-rhamnose 3'-o-methyltransferase, an enzyme in Calicheamicin biosynthesis

Replaces:  4PWR

Summary for 5HOQ

• Entry DOI: 10.2210/pdb5hoq/pdb
• Descriptor: TDP-rhamnose 3'-O-methyltransferase (CalS11), SULFATE ION (3 entities in total)
• Functional Keywords: rhamnose methyltransferase calicheamicin biosynthesis, transferase
• Biological source: Micromonospora echinospora
• Total number of polymer chains: 5
• Total formula weight: 145234.54

Authors

Han, L.,Helmich, K.E.,Singh, S.,Thorson, J.S.,Bingman, C.A.,Phillips Jr., G.N.,Enzyme Discovery for Natural Product Biosynthesis (deposition date: 2016-01-19, release date: 2016-03-30, Last modification date: 2023-09-27)

Primary citation

Han, L.,Singh, S.,Thorson, J.S.,Phillips, G.N.
Loop dynamics of thymidine diphosphate-rhamnose 3'-O-methyltransferase (CalS11), an enzyme in calicheamicin biosynthesis.
Struct Dyn., 3:012004-012004, 2016

PubMed Abstract: Structure analysis and ensemble refinement of the apo-structure of thymidine diphosphate (TDP)-rhamnose 3'-O-methyltransferase reveal a gate for substrate entry and product release. TDP-rhamnose 3'-O-methyltransferase (CalS11) catalyses a 3'-O-methylation of TDP-rhamnose, an intermediate in the biosynthesis of enediyne antitumor antibiotic calicheamicin. CalS11 operates at the sugar nucleotide stage prior to glycosylation step. Here, we present the crystal structure of the apo form of CalS11 at 1.89 Å resolution. We propose that the L2 loop functions as a gate facilitating and/or providing specificity for substrate entry or promoting product release. Ensemble refinement analysis slightly improves the crystallographic refinement statistics and furthermore provides a compelling way to visualize the dynamic model of loop L2, supporting the understanding of its proposed role in catalysis.

PubMed: 26958582
DOI: 10.1063/1.4941368

Experimental method

X-RAY DIFFRACTION (1.793 Å)