3V91

Structure of T82M glycogenin mutant truncated at residue 270 complexed with UDP-glucose

Summary for 3V91

• Entry DOI: 10.2210/pdb3v91/pdb
• Related: 1LL0 1LL2 1LL3 1ZCT 1ZCU 1ZCV 1ZCY 3V8Y 3V8Z 3V90
• Descriptor: Glycogenin-1, GLYCEROL, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: transferase
• Biological source: Oryctolagus cuniculus (European rabbit,Japanese white rabbit,domestic rabbit,rabbits)
• Total number of polymer chains: 1
• Total formula weight: 33386.55

Authors

Carrizo, M.E.,Romero, J.M.,Issoglio, F.M.,Curtino, J.A. (deposition date: 2011-12-23, release date: 2012-01-25, Last modification date: 2024-02-28)

Primary citation

Carrizo, M.E.,Romero, J.M.,Issoglio, F.M.,Curtino, J.A.
Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation.
Febs Lett., 586:254-257, 2012

PubMed Abstract: The X-ray structure of rabbit glycogenin containing the T82M (T83M according to previous authors amino acid numbering) mutation causing glycogenosis showed the loss of Thr82 hydrogen bond to Asp162, the residue involved in the activation step of the glucose transfer reaction mechanism. Autoglucosylation, maltoside transglucosylation and UDP-glucose hydrolyzing activities were abolished even though affinity and interactions with UDP-glucose and positioning of Tyr194 acceptor were conserved. Substitution of Thr82 for serine but not for valine restored the maximum extent of autoglucosylation as well as transglucosylation and UDP-glucose hydrolysis rate. Results provided evidence sustaining the essential role of the lost single hydrogen bond for UDP-glucose activation leading to glycogenin-bound glycogen primer synthesis.

PubMed: 22226635
DOI: 10.1016/j.febslet.2011.12.028

Experimental method

X-RAY DIFFRACTION (2 Å)