1bbu

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[[Image:1bbu.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1bbu| PDB=1bbu | SCENE= }}
{{STRUCTURE_1bbu| PDB=1bbu | SCENE= }}
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'''LYSYL-TRNA SYNTHETASE (LYSS) COMPLEXED WITH LYSINE'''
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===LYSYL-TRNA SYNTHETASE (LYSS) COMPLEXED WITH LYSINE===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11041850}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11041850 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11041850}}
==About this Structure==
==About this Structure==
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[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Protein biosynthesis]]
[[Category: Protein biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:18:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:47:21 2008''

Revision as of 15:47, 30 June 2008

Image:1bbu.png

Template:STRUCTURE 1bbu

LYSYL-TRNA SYNTHETASE (LYSS) COMPLEXED WITH LYSINE

Template:ABSTRACT PUBMED 11041850

About this Structure

1BBU 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

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