1e15
From Proteopedia
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| - | [[Image:1e15.gif|left|200px]] | + | [[Image:1e15.gif|left|200px]] |
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| - | '''CHITINASE B FROM SERRATIA MARCESCENS''' | + | {{Structure |
| + | |PDB= 1e15 |SIZE=350|CAPTION= <scene name='initialview01'>1e15</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CHITINASE B FROM SERRATIA MARCESCENS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E15 is a [ | + | 1E15 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10823940 10823940] |
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:47:51 2008'' |
Revision as of 08:47, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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