U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 6

1.

GLGE, C-terminal

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
Family Accession:
NF044853.2
Method:
HMM
2.

maltotransferase domain-containing protein

This entry represents domain N and S of GlgE. GlgE is a homodimer and a member of the GH13_3 CAZy subfamily. Each subunit of GlgE is composed of five domains, domain A is a (beta/alpha)8 barrel, typical of the catalytic domain of this family of enzymes, that forms part of the dimer interface. Domain B corresponds to an insertion after the third beta-strand of domain A [1]. In GlgE, domain B is fairly typical for a GH13 enzyme [2] in having a pair of anti-parallel strands and one short helix. The C-terminal domain C has a beta-sandwich fold. The N-terminal domain N, which also consists of a beta-sandwich fold, forms the core of the dimer interface. The final domain arises from an insertion within domain N and forms a four-helix bundle where the last helix is discontinuous and slightly kinked. This domain, which will henceforth be referred to as domain S, participates in the dimer interface and interacts directly with domain B of the neighbouring subunit [3]. [1]. 11257505. Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. MacGregor EA, Janecek S, Svensson B;. Biochim Biophys Acta. 2001;1546:1-20. [2]. 9302327. Domain evolution in the alpha-amylase family. Janecek S, Svensson B, Henrissat B;. J Mol Evol. 1997;45:322-331. [3]. 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. (from Pfam)

GO Terms:
Molecular Function:
hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553)
Date:
2024-10-16
Family Accession:
NF023324.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.

alpha-1,4-glucan--maltose-1-phosphate maltosyltransferase

alpha-1,4-glucan--maltose-1-phosphate maltosyltransferase uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans in the branched alpha-glucan biosynthetic pathway

Date:
2024-11-14
Family Accession:
10571012
Method:
Sparcle
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center