We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1bbw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bbw.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1bbw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bbw| PDB=1bbw | SCENE= }}
{{STRUCTURE_1bbw| PDB=1bbw | SCENE= }}
-
'''LYSYL-TRNA SYNTHETASE (LYSS)'''
+
===LYSYL-TRNA SYNTHETASE (LYSS)===
-
==Overview==
+
<!--
-
Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. A comparison between the unliganded and lysine-bound structures reveals major conformational changes upon lysine binding. The lysine substrate is involved in a network of hydrogen bonds. Two of these interactions, one between the alpha-amino group and the carbonyl oxygen of Gly 216 and the other between the carboxylate group and the side chain of Arg 262, trigger a subtle and complicated reorganization of the active site, involving the ordering of two loops (residues 215-217 and 444-455), a change in conformation of residues 393-409, and a rotation of a 4-helix bundle domain (located between motif 2 and 3) by 10 degrees. The result of these changes is a closing up of the active site upon lysine binding.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11041850}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11041850 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11041850}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Protein biosynthesis]]
[[Category: Protein biosynthesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:19:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:47:19 2008''

Revision as of 15:47, 30 June 2008

Image:1bbw.png


PDB ID 1bbw

Drag the structure with the mouse to rotate
1bbw, resolution 2.70Å ()
Gene: LYSS (Escherichia coli)
Activity: Lysine--tRNA ligase, with EC number 6.1.1.6
Related: 1bbu
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



LYSYL-TRNA SYNTHETASE (LYSS)

Template:ABSTRACT PUBMED 11041850

About this Structure

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

Reference

Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding., Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P, Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:11041850

Page seeded by OCA on Mon Jun 30 18:47:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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