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540 a.a.
Key reference
DOI no: 10.1107/S0907444902021923 Acta Crystallogr D Biol Crystallogr 59:400-403 (2003) PubMed id: 12554965
De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin. Y.Papanikolau, G.Tavlas, C.E.Vorgias, K.Petratos. ABSTRACT
The purification scheme of chitinase A (ChiA) from S. marcescens has been extensively revised. The pure enzyme crystallizes readily under new crystallization conditions. The ChiA crystal structure has been refined to 1.55 A resolution and the crystal structure of ChiA co-crystallized with the inhibitor allosamidin has been refined to 1.9 A resolution. Allosamidin is located in the deep active-site tunnel of ChiA and interacts with three important residues: Glu315, the proton donor of the catalysis, Asp313, which adopts two conformations in the native structure but is oriented towards Glu315 in the inhibitor complex, and Tyr390, which lies opposite Glu315 in the active-site tunnel.
Selected figure(s)
Figure 2.
Figure 2 ChiA-allosamidin complex. (a) Stereoview of the C^-atom trace of the enzyme molecule (green) with the inhibitor (red) bound to the active-site tunnel (PDB code [112]1ffq ). (b) Allosamidin in the electron density of the weighted 2F[o] - F[c] map contoured at 2 [113][sigma] (blue) and the neighbouring residues of ChiA. (c) Close-up view of allosamidin bound to the enzyme's active-site tunnel at subsites -1 to -3. The allosamizoline moiety fits into a local well.
The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 400-403) copyright 2003. Figure was selected by the author.
Literature references that cite this PDB file's key reference
PubMed id Reference
16685709 S.Pyrpassopoulos, M.Vlassi, A.Tsortos, Y.Papanikolau, K.Petratos, C.E.Vorgias, and G.Nounesis (2006).
Equilibrium heat-induced denaturation of chitinase 40 from Streptomyces thermoviolaceus.Proteins, 64, 513-523.
14717693 B.Synstad, S.Gåseidnes, D.M.Van Aalten, G.Vriend, J.E.Nielsen, and V.G.Eijsink (2004).
Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase.Eur J Biochem, 271, 253-262.
14597613 G.Vaaje-Kolstad, A.Vasella, M.G.Peter, C.Netter, D.R.Houston, B.Westereng, B.Synstad, V.G.Eijsink, and D.M.van Aalten (2004).
Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone.J Biol Chem, 279, 3612-3619.
PDB codes: 1ur8 1ur9 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 codes are shown on the right.
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