This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1iqq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1iqq.jpg|left|200px]]<br /><applet load="1iqq" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1iqq.jpg|left|200px]]
-
caption="1iqq, resolution 1.50&Aring;" />
+
 
-
'''Crystal Structure of Japanese pear S3-RNase'''<br />
+
{{Structure
 +
|PDB= 1iqq |SIZE=350|CAPTION= <scene name='initialview01'>1iqq</scene>, resolution 1.50&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_T(2) Ribonuclease T(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.1 3.1.27.1]
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal Structure of Japanese pear S3-RNase'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1IQQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrus_pyrifolia Pyrus pyrifolia]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(2) Ribonuclease T(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.1 3.1.27.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQQ OCA].
+
1IQQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrus_pyrifolia Pyrus pyrifolia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQQ OCA].
==Reference==
==Reference==
-
Crystal structure at 1.5-A resolution of Pyrus pyrifolia pistil ribonuclease responsible for gametophytic self-incompatibility., Matsuura T, Sakai H, Unno M, Ida K, Sato M, Sakiyama F, Norioka S, J Biol Chem. 2001 Nov 30;276(48):45261-9. Epub 2001 Sep 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11577107 11577107]
+
Crystal structure at 1.5-A resolution of Pyrus pyrifolia pistil ribonuclease responsible for gametophytic self-incompatibility., Matsuura T, Sakai H, Unno M, Ida K, Sato M, Sakiyama F, Norioka S, J Biol Chem. 2001 Nov 30;276(48):45261-9. Epub 2001 Sep 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11577107 11577107]
[[Category: Pyrus pyrifolia]]
[[Category: Pyrus pyrifolia]]
[[Category: Ribonuclease T(2)]]
[[Category: Ribonuclease T(2)]]
Line 24: Line 33:
[[Category: t2 family ribonuclease]]
[[Category: t2 family ribonuclease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:43 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:53:41 2008''

Revision as of 09:53, 20 March 2008


PDB ID 1iqq

Drag the structure with the mouse to rotate
, resolution 1.50Å
Activity: Ribonuclease T(2), with EC number 3.1.27.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Japanese pear S3-RNase


Overview

The crystal structure of the Pyrus pyrifolia pistil ribonuclease (S(3)-RNase) responsible for gametophytic self-incompatibility was determined at 1.5-A resolution. It consists of eight helices and seven beta-strands, and its folding topology is typical of RNase T(2) family enzymes. Based on a structural comparison of S(3)-RNase with RNase Rh, a fungal RNase T(2) family enzyme, the active site residues of S(3)-RNase assigned were His(33) and His(88) as catalysts and Glu(84) and Lys(87) as stabilizers of an intermediate in the transition state. Moreover, amino acid residues that constitute substrate binding sites of the two RNases could be superimposed geometrically. A hypervariable (HV) region that has an S-allele-specific sequence comprises a long loop and short alpha-helix. This region is far from the active site cleft, exposed on the molecule's surface, and positively charged. Four positively selected (PS) regions, in which the number of nonsynonymous substitutions exceeds that of synonymous ones, are located on either side of the active site cleft, and accessible to solvent. These structural features suggest that the HV or PS regions may interact with a pollen S-gene product(s) to recognize self and non-self pollen.

About this Structure

1IQQ is a Single protein structure of sequence from Pyrus pyrifolia. Full crystallographic information is available from OCA.

Reference

Crystal structure at 1.5-A resolution of Pyrus pyrifolia pistil ribonuclease responsible for gametophytic self-incompatibility., Matsuura T, Sakai H, Unno M, Ida K, Sato M, Sakiyama F, Norioka S, J Biol Chem. 2001 Nov 30;276(48):45261-9. Epub 2001 Sep 27. PMID:11577107

Page seeded by OCA on Thu Mar 20 11:53:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools