This entry represents the C-terminal domain of alpha-1,4-glucan:maltose-1-phosphate maltosyltransferases (GLGE) which has an all-beta fold [1-5]. This domain, referred to domain C, together with the catalytic one, is involved in the binding of alpha-glucan chains [4]. Paper describing PDB structure 3zss. [1]. 21914799. Structure of Streptomyces maltosyltransferase GlgE, a homologue of a genetically validated anti-tuberculosis target. Syson K, Stevenson CEM, Rejzek M, Fairhurst SA, Nair A, Bruton CJ, Field RA, Chater KF, Lawson DM, Bornemann S;. J Biol Chem. 2011;286:38298-38310. Paper describing PDB structure 4cn1. [2]. 24689960. Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds alpha-maltose 1-phosphate and forms a maltosyl-enzyme intermediate. Syson K, Stevenson CE, Rashid AM, Saalbach G, Tang M, Tuukkanen A, Svergun DI, Withers SG, Lawson DM, Bornemann S;. Biochemistry. 2014;53:2494-2504. Paper describing PDB structure 4u2y. [3]. 26245983. Crystal structures of Mycobacterium tuberculosis GlgE and complexes with non-covalent inhibitors. Lindenberger JJ, Veleti SK, Wilson BN, Sucheck SJ, Ronning DR;. Sci Rep. 2015;5:12830. Paper describing PDB structure 5cgm. [4]. 26616850. Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism. Mendes V, Blaszczyk M, Maranha A, Empadinhas N, Blundell TL;. Sci Rep. 2015;5:17144. Paper describing PDB structure 5cvs. [5]. 27531751. Ligand-bound Structures and Site-directed Mutagenesis Identify the Acceptor and Secondary Binding Sites of Streptomyces coelicolor Maltosyltransferase Glg. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-10-16