1edq: Difference between revisions

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[[Image:1edq.gif|left|200px]]<br /><applet load="1edq" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1edq.gif|left|200px]]<br /><applet load="1edq" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1edq, resolution 1.55Å" />

'''CRYSTAL STRUCTURE OF CHITINASE A FROM S. MARCESCENS AT 1.55 ANGSTROMS'''<br />

==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.

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==

1EDQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. 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=1EDQ OCA].

1EDQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. 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=1EDQ OCA].

==Reference==

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[[Category: beta-alpha (tim) barrel]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sat Nov 24 22~~:05:~~09 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:41 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1edq.gif|left|200px]]<br /><applet load="1edq" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1edq.gif|left|200px]]<br /><applet load="1edq" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1edq, resolution 1.55&Aring;" />
 '''CRYSTAL STRUCTURE OF CHITINASE A FROM S. MARCESCENS AT 1.55 ANGSTROMS'''<br />
 ==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.
+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==
-EDQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. 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=1EDQ OCA].
+EDQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. 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=1EDQ OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: beta-alpha (tim) barrel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:05:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:41 2008''