1e6z
CHITINASE B FROM SERRATIA MARCESCENS WILDTYPE IN COMPLEX WITH CATALYTIC INTERMEDIATE
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OverviewOverview
Chitinase B (ChiB) from Serratia marcescens is a family 18 exo-chitinase, whose catalytic domain has a TIM-barrel fold with a tunnel-shaped active, site. We have solved structures of three ChiB complexes that reveal, details of substrate binding, substrate-assisted catalysis, and product, displacement. The structure of an inactive ChiB mutant (E144Q) complexed, with a pentameric substrate (binding in subsites -2 to +3) shows closure, of the "roof" of the active site tunnel. It also shows that the sugar in, the -1 position is distorted to a boat conformation, thus providing, structural evidence in support of a previously proposed catalytic, mechanism. The structures of the active enzyme complexed to allosamidin, (an analogue of a proposed reaction intermediate) and of the active enzyme, ... [(full description)]
About this StructureAbout this Structure
1E6Z is a [Single protein] structure of sequence from [Serratia marcescens] with NAG, SO4 and NGO as [ligands]. Active as [[1]], with EC number [3.2.1.14]. Full crystallographic information is available from [OCA].
ReferenceReference
Structural insights into the catalytic mechanism of a family 18 exo-chitinase., van Aalten DM, Komander D, Synstad B, Gaseidnes S, Peter MG, Eijsink VG, Proc Natl Acad Sci U S A. 2001 Jul 31;98(16):8979-84. PMID:11481469
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