3b9e
From Proteopedia
Crystal structure of inactive mutant E315M chitinase A from Vibrio harveyi
Overview
This research describes four X-ray structures of Vibrio harveyi chitinase A and its catalytically inactive mutant (E315M) in the presence and absence of substrates. The overall structure of chitinase A is that of a typical family-18 glycosyl hydrolase comprising three distinct domains: (i) the amino-terminal chitin-binding domain; (ii) the main catalytic (alpha/beta)(8) TIM-barrel domain; and (iii) the small (alpha+beta) insertion domain. The catalytic cleft of chitinase A has a long, deep groove, which contains six chitooligosaccharide ring-binding subsites (-4)(-3)(-2)(-1)(+1)(+2). The binding cleft of the ligand-free E315M is partially blocked by the C-terminal (His)(6)-tag. Structures of E315M-chitooligosaccharide complexes display a linear conformation of pentaNAG, but a bent conformation of hexaNAG. Analysis of the final 2F(o)-F(c) omit map of E315M-NAG6 reveals the existence of the linear conformation of the hexaNAG at a lower occupancy with respect to the bent conformation. These crystallographic data provide evidence that the interacting sugars undergo conformational changes prior to hydrolysis by the wild-type enzyme.
About this Structure
3B9E is a Single protein structure of sequence from Vibrio harveyi. Full crystallographic information is available from OCA.
Reference
Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: implications for the catalytic mechanism., Songsiriritthigul C, Pantoom S, Aguda AH, Robinson RC, Suginta W, J Struct Biol. 2008 Jun;162(3):491-9. Epub 2008 Mar 26. PMID:18467126 Page seeded by OCA on Wed Jun 18 12:20:30 2008
