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481 a.a.
_CA
_NA
Key reference
DOI no: 10.1107/S0907444904027118 Acta Crystallogr D Biol Crystallogr 61:190-193 (2005) PubMed id: 15681870
Structure of a Bacillus halmapalus family 13 alpha-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 A resolution. G.J.Davies, A.M.Brzozowski, Z.Dauter, M.D.Rasmussen, T.V.Borchert, K.S.Wilson. ABSTRACT
The enzymatic digestion of starch by alpha-amylases is one of the key biotechnological reactions of recent times. In the search for industrial biocatalysts, the family GH13 alpha-amylase BHA from Bacillus halmapalus has been cloned and expressed. The three-dimensional structure at 2.1 A resolution has been determined in complex with the (pseudo)tetrasaccharide inhibitor acarbose. Acarbose is found bound as a nonasaccharide transglycosylation product spanning the -6 to +3 subsites. Careful inspection of electron density suggests that the bound ligand could not have been formed through successive transglycosylations of acarbose and must also have featured maltose or maltooligosaccharides as an acceptor.
Selected figure(s)
Figure 1.
Figure 1 (a) The covalent glycosyl-enzyme intermediate of a retaining glycosidase is normally intercepted by water. Under some circumstances, it is instead intercepted by another sugar in a transglycosylation reaction; such a mechanism gives rise to the many elongated forms of acarbose seen in amylase structures. (b) The structure of the pseudo-tetrasaccharide inhibitor acarbose. (c) The nonasaccharide observed in BHA (this work) and (d) that previously observed on the BA2-amylase (Brzozowski et al., 2000[Brzozowski, A. M., Lawson, D. M., Turkenburg, J. P., Bisgaard-Frantzen, H., Svendsen, A., Borchert, T. V., Dauter, Z., Wilson, K. S. & Davies, G. J. (2000). Biochemistry, 39, 9099-9107.]).
The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2005, 61, 190-193) copyright 2005. Figure was selected by an automated process.
Literature references that cite this PDB file's key reference
PubMed id Reference
17154418 T.Shirai, K.Igarashi, T.Ozawa, H.Hagihara, T.Kobayashi, K.Ozaki, and S.Ito (2007).
Ancestral sequence evolutionary trace and crystal structure analyses of alkaline alpha-amylase from Bacillus sp. KSM-1378 to clarify the alkaline adaptation process of proteins.Proteins, 66, 600-610.
PDB code: 2die 16946462 L.Lyhne-Iversen, T.J.Hobley, S.G.Kaasgaard, and P.Harris (2006).
Structure of Bacillus halmapalus alpha-amylase crystallized with and without the substrate analogue acarbose and maltose.Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 849-854.
PDB codes: 2gjp 2gjr
16452622 R.Kanai, K.Haga, T.Akiba, K.Yamane, and K.Harata (2006).
Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.Protein Sci, 15, 468-477.
PDB codes: 2d3l 2d3n
16030022 X.Robert, R.Haser, H.Mori, B.Svensson, and N.Aghajari (2005).
Oligosaccharide binding to barley alpha-amylase 1.J Biol Chem, 280, 32968-32978.
PDB codes: 1rp8 1rp9 1rpk The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.
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