1e15

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(New page: 200px<br /><applet load="1e15" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e15, resolution 1.90&Aring;" /> '''CHITINASE B FROM SER...)
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[[Image:1e15.gif|left|200px]]<br /><applet load="1e15" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1e15.gif|left|200px]]<br /><applet load="1e15" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1e15, resolution 1.90&Aring;" />
caption="1e15, resolution 1.90&Aring;" />
'''CHITINASE B FROM SERRATIA MARCESCENS'''<br />
'''CHITINASE B FROM SERRATIA MARCESCENS'''<br />
==Overview==
==Overview==
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In this paper, we describe the structure of chitinase B from Serratia, marcescens, which consists of a catalytic domain with a TIM-barrel fold, and a 49-residue C-terminal chitin-binding domain. This chitinase is the, first structure of a bacterial exochitinase, and it represents one of only, a few examples of a glycosyl hydrolase structure having interacting, catalytic and substrate-binding domains. The chitin-binding domain has, exposed aromatic residues that contribute to a 55-A long continuous, aromatic stretch extending into the active site. Binding of chitin, oligomers is blocked beyond the -3 subsite, which explains why the enzyme, has chitotriosidase activity and degrades the chitin chain from the, nonreducing end. Comparison of the chitinase B structure with that of, chitinase A explains why these enzymes act synergistically in the, degradation of chitin.
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In this paper, we describe the structure of chitinase B from Serratia marcescens, which consists of a catalytic domain with a TIM-barrel fold and a 49-residue C-terminal chitin-binding domain. This chitinase is the first structure of a bacterial exochitinase, and it represents one of only a few examples of a glycosyl hydrolase structure having interacting catalytic and substrate-binding domains. The chitin-binding domain has exposed aromatic residues that contribute to a 55-A long continuous aromatic stretch extending into the active site. Binding of chitin oligomers is blocked beyond the -3 subsite, which explains why the enzyme has chitotriosidase activity and degrades the chitin chain from the nonreducing end. Comparison of the chitinase B structure with that of chitinase A explains why these enzymes act synergistically in the degradation of chitin.
==About this Structure==
==About this Structure==
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1E15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E15 OCA].
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1E15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E15 OCA].
==Reference==
==Reference==
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[[Category: Serratia marcescens]]
[[Category: Serratia marcescens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Aalten, D.M.F.Van.]]
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[[Category: Aalten, D M.F Van.]]
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[[Category: Brurberg, M.B.]]
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[[Category: Brurberg, M B.]]
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[[Category: Eijsink, V.G.H.]]
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[[Category: Eijsink, V G.H.]]
[[Category: Hough, E.]]
[[Category: Hough, E.]]
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[[Category: Riise, B.W.]]
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[[Category: Riise, B W.]]
[[Category: Synstad, B.]]
[[Category: Synstad, B.]]
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[[Category: Wierenga, R.K.]]
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[[Category: Wierenga, R K.]]
[[Category: chitin degradation]]
[[Category: chitin degradation]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:55:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:42 2008''

Revision as of 10:22, 21 February 2008


1e15, resolution 1.90Å

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CHITINASE B FROM SERRATIA MARCESCENS

Overview

In this paper, we describe the structure of chitinase B from Serratia marcescens, which consists of a catalytic domain with a TIM-barrel fold and a 49-residue C-terminal chitin-binding domain. This chitinase is the first structure of a bacterial exochitinase, and it represents one of only a few examples of a glycosyl hydrolase structure having interacting catalytic and substrate-binding domains. The chitin-binding domain has exposed aromatic residues that contribute to a 55-A long continuous aromatic stretch extending into the active site. Binding of chitin oligomers is blocked beyond the -3 subsite, which explains why the enzyme has chitotriosidase activity and degrades the chitin chain from the nonreducing end. Comparison of the chitinase B structure with that of chitinase A explains why these enzymes act synergistically in the degradation of chitin.

About this Structure

1E15 is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.

Reference

Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution., van Aalten DM, Synstad B, Brurberg MB, Hough E, Riise BW, Eijsink VG, Wierenga RK, Proc Natl Acad Sci U S A. 2000 May 23;97(11):5842-7. PMID:10823940

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