3p0b

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Thermus thermophilus family GH57 branching enzyme: crystal structure, mechanism of action and products formed

Structural highlights

3p0b is a 1 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.35Å
Ligands:GOL
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BE_THET8 Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 3 to 13, with two local maxima at DP 7 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Is involved in glycogen biosynthesis. Shows a secondary activity, i.e. the hydrolysis of the substrate, being 4% of the total activity. Can use amylose as substrate but not alpha-1,4-linked oligosaccharides of 2-7 glucose residues, beta-cyclodextrin, 6-O-glucosyl-beta-cyclodextrin and 6-O-maltosyl-beta-cyclodextrin. Is not able to branch amylopectin further, it only hydrolyzes amylopectin. Thus, displays preference for linear and long substrates (amylose) over branched structures (amylopectin).[1]

References

  1. ↑ Palomo M, Pijning T, Booiman T, Dobruchowska JM, van der Vlist J, Kralj S, Planas A, Loos K, Kamerling JP, Dijkstra BW, van der Maarel MJ, Dijkhuizen L, Leemhuis H. Thermus thermophilus glycoside hydrolase family 57 branching enzyme: crystal structure, mechanism of action, and products formed. J Biol Chem. 2011 Feb 4;286(5):3520-30. Epub 2010 Nov 19. PMID:21097495 doi:http://dx.doi.org/10.1074/jbc.M110.179515

Contents


PDB ID 3p0b

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