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| [[Image:1bbu.gif|left|200px]] | | {{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'''
| | ===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.
| | 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. |
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| | {{ABSTRACT_PUBMED_11041850}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ligase]] | | [[Category: Ligase]] |
| [[Category: Protein biosynthesis]] | | [[Category: Protein biosynthesis]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:18:59 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:47:21 2008'' |
