6APL

Crystal Structure of human ST6GALNAC2 in complex with CMP

Summary for 6APL

• Entry DOI: 10.2210/pdb6apl/pdb
• Descriptor: Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2, CYTIDINE-5'-MONOPHOSPHATE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: glycosyltransferase, transferase, structural genomics, psi-biology, northeast structural genomics consortium, nesg
• Biological source: Homo sapiens (Human)
• Cellular location: Golgi apparatus membrane ; Single-pass type II membrane protein : Q9UJ37
• Total number of polymer chains: 6
• Total formula weight: 257780.12

Authors

Forouhar, F.,Moremen, K.W.,Northeast Structural Genomics Consortium (NESG),Tong, L. (deposition date: 2017-08-17, release date: 2017-12-20, Last modification date: 2024-11-20)

Primary citation

Moremen, K.W.,Ramiah, A.,Stuart, M.,Steel, J.,Meng, L.,Forouhar, F.,Moniz, H.A.,Gahlay, G.,Gao, Z.,Chapla, D.,Wang, S.,Yang, J.Y.,Prabhakar, P.K.,Johnson, R.,Rosa, M.D.,Geisler, C.,Nairn, A.V.,Seetharaman, J.,Wu, S.C.,Tong, L.,Gilbert, H.J.,LaBaer, J.,Jarvis, D.L.
Expression system for structural and functional studies of human glycosylation enzymes.
Nat. Chem. Biol., 14:156-162, 2018

PubMed Abstract: Vertebrate glycoproteins and glycolipids are synthesized in complex biosynthetic pathways localized predominantly within membrane compartments of the secretory pathway. The enzymes that catalyze these reactions are exquisitely specific, yet few have been extensively characterized because of challenges associated with their recombinant expression as functional products. We used a modular approach to create an expression vector library encoding all known human glycosyltransferases, glycoside hydrolases, and sulfotransferases, as well as other glycan-modifying enzymes. We then expressed the enzymes as secreted catalytic domain fusion proteins in mammalian and insect cell hosts, purified and characterized a subset of the enzymes, and determined the structure of one enzyme, the sialyltransferase ST6GalNAcII. Many enzymes were produced at high yields and at similar levels in both hosts, but individual protein expression levels varied widely. This expression vector library will be a transformative resource for recombinant enzyme production, broadly enabling structure-function studies and expanding applications of these enzymes in glycochemistry and glycobiology.

PubMed: 29251719
DOI: 10.1038/nchembio.2539

Experimental method

X-RAY DIFFRACTION (2.35 Å)