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From Proteopedia
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CHITINASE B FROM SERRATIA MARCESCENS MUTANT D142N IN COMPLEX WITH INHIBITOR ALLOSAMIDIN
Overview
Catalysis by ChiB, a family 18 chitinase from Serratia marcescens, involves a conformational change of Asp142 which is part of a, characteristic D(140)XD(142)XE(144) sequence motif. In the free enzyme, Asp142 points towards Asp140, whereas it rotates towards the catalytic, acid, Glu144, upon ligand binding. Mutation of Asp142 to Asn reduced, k(cat) and affinity for allosamidin, a competitive inhibitor. The X-ray, structure of the D142N mutant showed that Asn142 points towards Glu144 in, the absence of a ligand. The active site also showed other structural, adjustments (Tyr10, Ser93) that had previously been observed in the, wild-type enzyme upon substrate binding. The X-ray structure of a complex, of D142N with allosamidin, a pseudotrisaccharide competitive inhibitor, was essentially ... [(full description)]
About this Structure
1OGG is a [Single protein] structure of sequence from [Serratia marcescens] with SO4, AMI and GOL as [ligands]. Active as [[1]], with EC number [3.2.1.14]. Full crystallographic information is available from [OCA].
Reference
Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin., Vaaje-Kolstad G, Houston DR, Rao FV, Peter MG, Synstad B, van Aalten DM, Eijsink VG, Biochim Biophys Acta. 2004 Jan 14;1696(1):103-11. PMID:14726210
Page seeded by OCA on Mon Oct 29 21:15:32 2007
