1bbw
From Proteopedia
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| - | [[Image:1bbw.jpg|left|200px]] | + | [[Image:1bbw.jpg|left|200px]] |
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| - | '''LYSYL-TRNA SYNTHETASE (LYSS)''' | + | {{Structure |
| + | |PDB= 1bbw |SIZE=350|CAPTION= <scene name='initialview01'>1bbw</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Lysine--tRNA_ligase Lysine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.6 6.1.1.6] | ||
| + | |GENE= LYSS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''LYSYL-TRNA SYNTHETASE (LYSS)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BBW is a [ | + | 1BBW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11041850 11041850] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Lysine--tRNA ligase]] | [[Category: Lysine--tRNA ligase]] | ||
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[[Category: protein biosynthesis]] | [[Category: protein biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:08:54 2008'' |
Revision as of 08:08, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Gene: | LYSS (Escherichia coli) | ||||||
| Activity: | Lysine--tRNA ligase, with EC number 6.1.1.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
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
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