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.


2e1b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2e1b.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2e1b.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2e1b| PDB=2e1b | SCENE= }}
{{STRUCTURE_2e1b| PDB=2e1b | SCENE= }}
-
'''Crystal structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii'''
+
===Crystal structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii===
-
==Overview==
+
<!--
-
The editing domain of alanyl-tRNA synthetase (AlaRS) contributes to high-fidelity aminoacylation by hydrolyzing (editing) the incorrect products Ser-tRNA(Ala) and Gly-tRNA(Ala) (cis-editing). The AlaX protein shares sequence homology to the editing domain of AlaRS. There are three types of AlaX proteins, with different numbers of amino-acid residues (AlaX-S, AlaX-M and AlaX-L). In this report, AlaX-M from Pyrococcus horikoshii is shown to deacylate Ser-tRNA(Ala) and Gly-tRNA(Ala) (trans-editing). The crystal structure of P. horikoshii AlaX-M has been determined at 2.7 A resolution. AlaX-M consists of an N-terminal domain (N-domain) and a C-terminal domain (C-domain). A zinc ion is coordinated by the conserved zinc-binding cluster in the C-domain, which is expected to be the enzymatic active site. The glycine-rich motif, consisting of successive conserved glycine residues in the N-domain, forms a loop (the 'glycine-rich loop'). The glycine-rich loop is located near the active site and may be involved in substrate recognition and/or catalysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17327676}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17327676 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17327676}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Trans-editing enzyme]]
[[Category: Trans-editing enzyme]]
[[Category: Zinc-binding motif]]
[[Category: Zinc-binding motif]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:44:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:46:31 2008''

Revision as of 08:46, 29 July 2008

Template:STRUCTURE 2e1b

Crystal structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii

Template:ABSTRACT PUBMED 17327676

About this Structure

2E1B is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii., Fukunaga R, Yokoyama S, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):390-400. Epub 2007, Feb 21. PMID:17327676

Page seeded by OCA on Tue Jul 29 11:46:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools