1nj2

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[[Image:1nj2.gif|left|200px]]
[[Image:1nj2.gif|left|200px]]
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{{Structure
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|PDB= 1nj2 |SIZE=350|CAPTION= <scene name='initialview01'>1nj2</scene>, resolution 3.11&Aring;
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The line below this paragraph, containing "STRUCTURE_1nj2", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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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/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= MTH611 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 Methanothermobacter thermautotrophicus])
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|DOMAIN=
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{{STRUCTURE_1nj2| PDB=1nj2 | SCENE= }}
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|RELATEDENTRY=[[1nj1|1NJ1]], [[1nj5|1NJ5]], [[1nj6|1NJ6]], [[1nj8|1NJ8]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nj2 OCA], [http://www.ebi.ac.uk/pdbsum/1nj2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nj2 RCSB]</span>
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}}
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'''Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus'''
'''Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus'''
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[[Category: Steitz, T A.]]
[[Category: Steitz, T A.]]
[[Category: Wang, J.]]
[[Category: Wang, J.]]
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[[Category: class-ii trna synthetase]]
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[[Category: Class-ii trna synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:35:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:31:04 2008''
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Revision as of 23:35, 2 May 2008

Template:STRUCTURE 1nj2

Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus


Overview

Cysteinyl-tRNA synthetase is an essential enzyme required for protein synthesis. Genes encoding this protein have not been identified in Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus, or Methanopyrus kandleri. It has previously been proposed that the prolyl-tRNA synthetase (ProRS) enzymes in these organisms recognize either proline or cysteine and can aminoacylate their cognate tRNAs through a dual-specificity mechanism. We report five crystal structures at resolutions between 2.6 and 3.2 A: apo M. jannaschii ProRS, and M. thermautotrophicus ProRS in apo form and in complex with cysteinyl-sulfamoyl-, prolyl-sulfamoyl-, and alanyl-sulfamoyl-adenylates. These aminoacyl-adenylate analogues bind to a single active-site pocket and induce an identical set of conformational changes in loops around the active site when compared with the ligand-free conformation of ProRS. The cysteinyl- and prolyl-adenylate analogues have similar, nanomolar affinities for M. thermautotrophicus ProRS. Homology modeling of tRNA onto these adenylate complexes places the 3'-OH of A76 in an appropriate position for the transfer of any of the three amino acids to tRNA. Thus, these structures explain recent biochemical experiments showing that M. jannaschii ProRS misacylates tRNA(Pro) with cysteine, and argue against the proposal that these archaeal ProRS enzymes possess the dual capacity to aminoacylate both tRNA(Pro) and tRNA(Cys) with their cognate amino acids.

About this Structure

1NJ2 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

Reference

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases., Kamtekar S, Kennedy WD, Wang J, Stathopoulos C, Soll D, Steitz TA, Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1673-8. Epub 2003 Feb 10. PMID:12578991 Page seeded by OCA on Sat May 3 02:35:34 2008

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