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| {{STRUCTURE_3b9e| PDB=3b9e | SCENE= }} | | {{STRUCTURE_3b9e| PDB=3b9e | SCENE= }} |
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| '''Crystal structure of inactive mutant E315M chitinase A from Vibrio harveyi'''
| | ===Crystal structure of inactive mutant E315M chitinase A from Vibrio harveyi=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18467126}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18467126 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18467126}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| [[Category: Tim-barrel]] | | [[Category: Tim-barrel]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:20:30 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:58:43 2008'' |
