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.


1xty

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xty.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xty.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xty| PDB=1xty | SCENE= }}
{{STRUCTURE_1xty| PDB=1xty | SCENE= }}
-
'''Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase'''
+
===Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase===
-
==Overview==
+
<!--
-
The 3-D structure of the peptidyl-tRNA hydrolase from the archaea Sulfolobus solfataricus has been solved at 1.8 A resolution. Homologues of this enzyme are found in archaea and eucarya. Bacteria display a different type of peptidyl-tRNA hydrolase that is also encountered in eucarya. In solution, the S. solfataricus hydrolase behaves as a dimer. In agreement, the crystalline structure of this enzyme indicates the formation of a dimer. Each protomer is made of a mixed five-stranded beta-sheet surrounded by two groups of two alpha-helices. The dimer interface is mainly formed by van der Waals interactions between hydrophobic residues belonging to the two N-terminal alpha1 helices contributed by two protomers. Site-directed mutagenesis experiments were designed for probing the basis of specificity of the archaeal hydrolase. Among the strictly conserved residues within the archaeal/eucaryal peptidyl-tRNA hydrolase family, three residues, K18, D86, and T90, appear of utmost importance for activity. They are located in the N-part of alpha1 and in the beta3-beta4 loop. K18 and D86, which form a salt bridge, might play a role in the catalysis thanks to their acid and basic functions, whereas the OH group of T90 could act as a nucleophile. These observations clearly distinguish the active site of the archaeal/eucaryal hydrolases from that of the bacterial/eucaryal ones, where a histidine is believed to serve as the catalytic base.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15766258}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15766258 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15766258}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Schmitt, E.]]
[[Category: Schmitt, E.]]
[[Category: Mixed beta sheet]]
[[Category: Mixed beta sheet]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:30:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:40:26 2008''

Revision as of 13:40, 29 July 2008

Image:1xty.png

Template:STRUCTURE 1xty

Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase

Template:ABSTRACT PUBMED 15766258

About this Structure

1XTY is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.

Reference

Crystal structure at 1.8 A resolution and identification of active site residues of Sulfolobus solfataricus peptidyl-tRNA hydrolase., Fromant M, Schmitt E, Mechulam Y, Lazennec C, Plateau P, Blanquet S, Biochemistry. 2005 Mar 22;44(11):4294-301. PMID:15766258

Page seeded by OCA on Tue Jul 29 16:40:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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