PF11896

Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase, domain N/S

Pfam entry
Member databasePfam
Pfam typefamily
Short nameGlgE_dom_N_S
ClanE-set
Author Assefa S;0000-0003-2178-533X Coggill P;0000-0001-5731-1588 Bateman A;0000-0002-6982-4660
Sequence Ontology0100021

Description

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
[2]
. In GlgE, domain B is fairly typical for a GH13 enzyme
[3]
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
[1]
.

References

1.Structure of Streptomyces maltosyltransferase GlgE, a homologue of a genetically validated anti-tuberculosis target. Syson K, Stevenson CE, Rejzek M, Fairhurst SA, Nair A, Bruton CJ, Field RA, Chater KF, Lawson DM, Bornemann S. J. Biol. Chem. 286, 38298-310, (2011). View articlePMID: 21914799

2.Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. MacGregor EA, Janecek S, Svensson B. Biochim. Biophys. Acta 1546, 1-20, (2001). View articlePMID: 11257505

3.Domain evolution in the alpha-amylase family. Janecek S, Svensson B, Henrissat B. J. Mol. Evol. 45, 322-31, (1997). View articlePMID: 9302327

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