1nj5
From Proteopedia
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| - | [[Image:1nj5.gif|left|200px]] | + | [[Image:1nj5.gif|left|200px]] |
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| - | '''Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus bound to proline sulfamoyl adenylate''' | + | {{Structure |
| + | |PDB= 1nj5 |SIZE=350|CAPTION= <scene name='initialview01'>1nj5</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=P5A:'5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE'>P5A</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= MTH611 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 Methanothermobacter thermautotrophicus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus bound to proline sulfamoyl adenylate''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NJ5 is a [ | + | 1NJ5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJ5 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12578991 12578991] |
[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Proline--tRNA ligase]] | [[Category: Proline--tRNA ligase]] | ||
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[[Category: protein-aminoacyladenylate complex class-ii trna synthetase]] | [[Category: protein-aminoacyladenylate complex class-ii trna synthetase]] | ||
| - | ''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 12:57:34 2008'' |
Revision as of 10:57, 20 March 2008
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| , resolution 2.80Å | |||||||
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| Ligands: | , and | ||||||
| Gene: | MTH611 (Methanothermobacter thermautotrophicus) | ||||||
| Activity: | Proline--tRNA ligase, with EC number 6.1.1.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus bound to proline sulfamoyl adenylate
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
1NJ5 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
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