The effects of the surface-exposed residues on the binding and hydrolytic activities of chitinase A-0

Ligned with the -terminal fragment (residues 648–699), covering the ChBD of WL-12 chitinase A1. B) An alignment of the catalytic domain of the three bacterial chitinases with residues 160 to 289 of chitinase A being displayed. The chitinase sequences were retrieved from the Swiss-Prot/TreEMBL protein databases, aligned using "MegAlign" in the DNASTAR package, and displayed in Genedoc. The secondary structure of chitinase A was predicted from the PHD method in PredictProtein using as template [see texts]. Conserved residues are shaded in blue, whereas the residues that are aligned with Ser33, Trp70, Trp231, and Tyr245 of chitinase A are shaded in red. ChiA_Vibca: chitinase A (Q9AMP1), ChiA_Serma: chitinase A (P07254), and ChiA1_Bacc: chitinase A1 (P20533). -strand is represented by an arrow, -helix by a cylinder and loop by a straight line.<p><b>Copyright information:</b></p><p>Taken from "The effects of the surface-exposed residues on the binding and hydrolytic activities of chitinase A"</p><p>http://www.biomedcentral.com/1471-2091/9/2</p><p>BMC Biochemistry 2008;9():2-2.</p><p>Published online 21 Jan 2008</p><p>PMCID:PMC2265269.</p><p>