1ch0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ch0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ch0, resolution 2.3&Aring;" /> '''RNASE T1 VARIANT WITH...)
Line 1: Line 1:
-
[[Image:1ch0.jpg|left|200px]]<br /><applet load="1ch0" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ch0.jpg|left|200px]]<br /><applet load="1ch0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ch0, resolution 2.3&Aring;" />
caption="1ch0, resolution 2.3&Aring;" />
'''RNASE T1 VARIANT WITH ALTERED GUANINE BINDING SEGMENT'''<br />
'''RNASE T1 VARIANT WITH ALTERED GUANINE BINDING SEGMENT'''<br />
==Overview==
==Overview==
-
The ribonuclease T1 variant 9/5 with a guanine recognition segment, altered from the wild-type amino acid sequence 41-KYNNYE-46 to, 41-EFRNWQ-46, has been cocrystallised with the specific inhibitor 2'-GMP., The crystal structure has been refined to a crystallographic R factor of, 0.198 at 2.3 A resolution. Despite a size reduction of the binding pocket, pushing the inhibitor outside by 1 A, 2'-GMP is fixed to the primary, recognition site due to increased aromatic stacking interactions. The, phosphate group of 2'-GMP is located about 4.2 A apart from its position, in wild-type ribonuclease T1-2'-GMP complexes, allowing a Ca(2+), coordinating this phosphate group, to enter the binding pocket. The, crystallographic data can be aligned with the kinetic characterisation of, the variant, showing a reduction of both, guanine affinity and turnover, rate. The presence of Ca(2+) was shown to inhibit variant 9/5 and, wild-type enzyme to nearly the same extent.
+
The ribonuclease T1 variant 9/5 with a guanine recognition segment, altered from the wild-type amino acid sequence 41-KYNNYE-46 to 41-EFRNWQ-46, has been cocrystallised with the specific inhibitor 2'-GMP. The crystal structure has been refined to a crystallographic R factor of 0.198 at 2.3 A resolution. Despite a size reduction of the binding pocket, pushing the inhibitor outside by 1 A, 2'-GMP is fixed to the primary recognition site due to increased aromatic stacking interactions. The phosphate group of 2'-GMP is located about 4.2 A apart from its position in wild-type ribonuclease T1-2'-GMP complexes, allowing a Ca(2+), coordinating this phosphate group, to enter the binding pocket. The crystallographic data can be aligned with the kinetic characterisation of the variant, showing a reduction of both, guanine affinity and turnover rate. The presence of Ca(2+) was shown to inhibit variant 9/5 and wild-type enzyme to nearly the same extent.
==About this Structure==
==About this Structure==
-
1CH0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with CA, CL and 2GP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CH0 OCA].
+
1CH0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=2GP:'>2GP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CH0 OCA].
==Reference==
==Reference==
Line 25: Line 25:
[[Category: ribonuclease]]
[[Category: ribonuclease]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:26:45 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:02 2008''

Revision as of 10:06, 21 February 2008

Image:1ch0.jpg

1ch0, resolution 2.3Å

Drag the structure with the mouse to rotate

RNASE T1 VARIANT WITH ALTERED GUANINE BINDING SEGMENT

Overview

The ribonuclease T1 variant 9/5 with a guanine recognition segment, altered from the wild-type amino acid sequence 41-KYNNYE-46 to 41-EFRNWQ-46, has been cocrystallised with the specific inhibitor 2'-GMP. The crystal structure has been refined to a crystallographic R factor of 0.198 at 2.3 A resolution. Despite a size reduction of the binding pocket, pushing the inhibitor outside by 1 A, 2'-GMP is fixed to the primary recognition site due to increased aromatic stacking interactions. The phosphate group of 2'-GMP is located about 4.2 A apart from its position in wild-type ribonuclease T1-2'-GMP complexes, allowing a Ca(2+), coordinating this phosphate group, to enter the binding pocket. The crystallographic data can be aligned with the kinetic characterisation of the variant, showing a reduction of both, guanine affinity and turnover rate. The presence of Ca(2+) was shown to inhibit variant 9/5 and wild-type enzyme to nearly the same extent.

About this Structure

1CH0 is a Single protein structure of sequence from Aspergillus oryzae with , and as ligands. Active as Ribonuclease T(1), with EC number 3.1.27.3 Full crystallographic information is available from OCA.

Reference

Structural analysis of an RNase T1 variant with an altered guanine binding segment., Hoschler K, Hoier H, Hubner B, Saenger W, Orth P, Hahn U, J Mol Biol. 1999 Dec 17;294(5):1231-8. PMID:10600381

Page seeded by OCA on Thu Feb 21 12:06:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ch0"
Personal tools