2Z86

Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP

Summary for 2Z86

• Entry DOI: 10.2210/pdb2z86/pdb
• Descriptor: Chondroitin synthase, URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: gt-a, glycosyltransferase a, fold, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 293738.10

Authors

Osawa, T.,Sugiura, N.,Shimada, H.,Hirooka, R.,Tsuji, A.,Kimura, M.,Kimata, K.,Kakuta, Y. (deposition date: 2007-09-03, release date: 2008-09-16, Last modification date: 2024-03-13)

Primary citation

Osawa, T.,Sugiura, N.,Shimada, H.,Hirooka, R.,Tsuji, A.,Shirakawa, T.,Fukuyama, K.,Kimura, M.,Kimata, K.,Kakuta, Y.
Crystal structure of chondroitin polymerase from Escherichia coli K4.
Biochem. Biophys. Res. Commun., 378:10-14, 2009

PubMed Abstract: Elongation of glycosaminoglycan chains, such as heparan and chondroitin, is catalyzed by bi-functional glycosyltransferases, for which both 3-dimensional structures and reaction mechanisms remain unknown. The bacterial chondroitin polymerase K4CP catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. Here, we have determined the crystal structure of K4CP in the presence of UDP and UDP-GalNAc as well as with UDP and UDP-GlcUA. The structures consisted of two GT-A fold domains in which the two active sites were 60A apart. UDP-GalNAc and UDP-GlcUA were found at the active sites of the N-terminal and C-terminal domains, respectively. The present K4CP structures have provided the structural basis for further investigating the molecular mechanism of biosynthesis of chondroitin chain.

PubMed: 18771653
DOI: 10.1016/j.bbrc.2008.08.121

Experimental method

X-RAY DIFFRACTION (2.4 Å)