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.


1li7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1li7.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1li7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1li7| PDB=1li7 | SCENE= }}
{{STRUCTURE_1li7| PDB=1li7 | SCENE= }}
-
'''Crystal Structure of Cysteinyl-tRNA Synthetase with Cysteine Substrate Bound'''
+
===Crystal Structure of Cysteinyl-tRNA Synthetase with Cysteine Substrate Bound===
-
==Overview==
+
<!--
-
Cysteinyl-tRNA synthetase (CysRS) is highly specific for synthesis of cysteinyl adenylate, yet does not possess the amino acid editing activity characteristic of many other tRNA synthetases. To elucidate how CysRS is able to distinguish cysteine from non-cognate amino acids, crystal structures of the Escherichia coli enzyme were determined in apo and cysteine-bound states. The structures reveal that the substrate cysteine thiolate forms a single direct interaction with a zinc ion bound at the base of the active site cleft, in a trigonal bipyramidal geometry together with four highly conserved protein side chains. Cysteine binding induces movement of the zinc ion towards substrate, as well as flipping of the conserved Trp205 indole ring to pack on the thiol side chain. The imidazole groups of five conserved histidines lie adjacent to the zinc ion, forming a unique arrangement suggestive of functional significance. Thus, amino acid discrimination without editing arises most directly from the favorable zinc-thiolate interaction, which is not possible for non-cognate substrates. Additional selectivity may be generated during the induced-fit conformational changes that help assemble the active site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12032090}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12032090 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12032090}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: E coli]]
[[Category: E coli]]
[[Category: Trna synthetase]]
[[Category: Trna synthetase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:56:50 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:57:59 2008''

Revision as of 17:58, 2 July 2008

Image:1li7.png

Template:STRUCTURE 1li7

Crystal Structure of Cysteinyl-tRNA Synthetase with Cysteine Substrate Bound

Template:ABSTRACT PUBMED 12032090

About this Structure

1LI7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase., Newberry KJ, Hou YM, Perona JJ, EMBO J. 2002 Jun 3;21(11):2778-87. PMID:12032090

Page seeded by OCA on Wed Jul 2 20:57:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1li7"
Personal tools