1goi
From Proteopedia
(New page: 200px<br /><applet load="1goi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1goi, resolution 1.45Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1goi.gif|left|200px]]<br /><applet load="1goi" size=" | + | [[Image:1goi.gif|left|200px]]<br /><applet load="1goi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1goi, resolution 1.45Å" /> | caption="1goi, resolution 1.45Å" /> | ||
'''CRYSTAL STRUCTURE OF THE D140N MUTANT OF CHITINASE B FROM SERRATIA MARCESCENS AT 1.45 A RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF THE D140N MUTANT OF CHITINASE B FROM SERRATIA MARCESCENS AT 1.45 A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the inactive D140N mutant of Serratia marcescens | + | The crystal structure of the inactive D140N mutant of Serratia marcescens was refined to 1.45 A resolution. The structure of the mutant was essentially identical to that of the wild type, with the exception of a rotation of Asp142 in the catalytic centre. In the mutant, this residue interacts with the catalytic acid (Glu144) and not with residue 140 as in the wild type. Thus, the 500-fold decrease in activity in the D140N mutant seems to be largely mediated by an effect on Asp142, confirming the crucial role of the latter residue in catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1GOI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] Full crystallographic information is available from [http:// | + | 1GOI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Aalten, D | + | [[Category: Aalten, D M.F Van.]] |
| - | [[Category: Eijsink, V | + | [[Category: Eijsink, V G.H.]] |
[[Category: Kolstad, G.]] | [[Category: Kolstad, G.]] | ||
[[Category: Synstad, B.]] | [[Category: Synstad, B.]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:18 2008'' |
Revision as of 10:52, 21 February 2008
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CRYSTAL STRUCTURE OF THE D140N MUTANT OF CHITINASE B FROM SERRATIA MARCESCENS AT 1.45 A RESOLUTION
Overview
The crystal structure of the inactive D140N mutant of Serratia marcescens was refined to 1.45 A resolution. The structure of the mutant was essentially identical to that of the wild type, with the exception of a rotation of Asp142 in the catalytic centre. In the mutant, this residue interacts with the catalytic acid (Glu144) and not with residue 140 as in the wild type. Thus, the 500-fold decrease in activity in the D140N mutant seems to be largely mediated by an effect on Asp142, confirming the crucial role of the latter residue in catalysis.
About this Structure
1GOI is a Single protein structure of sequence from Serratia marcescens with and as ligands. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.
Reference
Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution., Kolstad G, Synstad B, Eijsink VG, van Aalten DM, Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):377-9. Epub 2002, Jan 24. PMID:11807282
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