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1bbw

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[[Image:1bbw.jpg|left|200px]]
[[Image:1bbw.jpg|left|200px]]
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{{Structure
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|PDB= 1bbw |SIZE=350|CAPTION= <scene name='initialview01'>1bbw</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1bbw", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE= LYSS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1bbw| PDB=1bbw | SCENE= }}
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|RELATEDENTRY=[[1bbu|1BBU]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbw OCA], [http://www.ebi.ac.uk/pdbsum/1bbw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bbw RCSB]</span>
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'''LYSYL-TRNA SYNTHETASE (LYSS)'''
'''LYSYL-TRNA SYNTHETASE (LYSS)'''
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[[Category: Onesti, S.]]
[[Category: Onesti, S.]]
[[Category: Plateau, P.]]
[[Category: Plateau, P.]]
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[[Category: aminoacyl-trna synthetase]]
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[[Category: Aminoacyl-trna synthetase]]
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[[Category: ligase]]
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[[Category: Ligase]]
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[[Category: protein biosynthesis]]
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[[Category: Protein biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:19:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:57:46 2008''
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Revision as of 08:19, 2 May 2008

Image:1bbw.jpg


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)


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 Page seeded by OCA on Fri May 2 11:19:03 2008

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