1ffq

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(New page: 200px<br /><applet load="1ffq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ffq, resolution 1.9&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1ffq.gif|left|200px]]<br /><applet load="1ffq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ffq, resolution 1.9&Aring;" />
caption="1ffq, resolution 1.9&Aring;" />
'''CRYSTAL STRUCTURE OF CHITINASE A COMPLEXED WITH ALLOSAMIDIN'''<br />
'''CRYSTAL STRUCTURE OF CHITINASE A COMPLEXED WITH ALLOSAMIDIN'''<br />
==Overview==
==Overview==
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The purification scheme of chitinase A (ChiA) from S. marcescens has been, extensively revised. The pure enzyme crystallizes readily under new, crystallization conditions. The ChiA crystal structure has been refined to, 1.55 A resolution and the crystal structure of ChiA co-crystallized with, the inhibitor allosamidin has been refined to 1.9 A resolution., Allosamidin is located in the deep active-site tunnel of ChiA and, interacts with three important residues: Glu315, the proton donor of the, catalysis, Asp313, which adopts two conformations in the native structure, but is oriented towards Glu315 in the inhibitor complex, and Tyr390, which, lies opposite Glu315 in the active-site tunnel.
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The purification scheme of chitinase A (ChiA) from S. marcescens has been extensively revised. The pure enzyme crystallizes readily under new crystallization conditions. The ChiA crystal structure has been refined to 1.55 A resolution and the crystal structure of ChiA co-crystallized with the inhibitor allosamidin has been refined to 1.9 A resolution. Allosamidin is located in the deep active-site tunnel of ChiA and interacts with three important residues: Glu315, the proton donor of the catalysis, Asp313, which adopts two conformations in the native structure but is oriented towards Glu315 in the inhibitor complex, and Tyr390, which lies opposite Glu315 in the active-site tunnel.
==About this Structure==
==About this Structure==
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1FFQ 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 AMI as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FFQ OCA].
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1FFQ 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=AMI:'>AMI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1FFQ OCA].
==Reference==
==Reference==
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[[Category: Petratos, K.]]
[[Category: Petratos, K.]]
[[Category: Tavlas, G.]]
[[Category: Tavlas, G.]]
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[[Category: Vorgias, C.E.]]
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[[Category: Vorgias, C E.]]
[[Category: AMI]]
[[Category: AMI]]
[[Category: enzyme-inhibitor complex]]
[[Category: enzyme-inhibitor complex]]
[[Category: glycosyl hydrolase]]
[[Category: glycosyl hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:53:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:11 2008''

Revision as of 10:38, 21 February 2008


1ffq, resolution 1.9Å

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CRYSTAL STRUCTURE OF CHITINASE A COMPLEXED WITH ALLOSAMIDIN

Overview

The purification scheme of chitinase A (ChiA) from S. marcescens has been extensively revised. The pure enzyme crystallizes readily under new crystallization conditions. The ChiA crystal structure has been refined to 1.55 A resolution and the crystal structure of ChiA co-crystallized with the inhibitor allosamidin has been refined to 1.9 A resolution. Allosamidin is located in the deep active-site tunnel of ChiA and interacts with three important residues: Glu315, the proton donor of the catalysis, Asp313, which adopts two conformations in the native structure but is oriented towards Glu315 in the inhibitor complex, and Tyr390, which lies opposite Glu315 in the active-site tunnel.

About this Structure

1FFQ is a Single protein structure of sequence from Serratia marcescens with as ligand. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.

Reference

De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin., Papanikolau Y, Tavlas G, Vorgias CE, Petratos K, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):400-3. Epub 2003, Jan 23. PMID:12554965

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