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New page: left|200px<br /><applet load="1nj8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nj8, resolution 3.20Å" /> '''Crystal Structure of...
 
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[[Image:1nj8.gif|left|200px]]<br /><applet load="1nj8" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1nj8, resolution 3.20&Aring;" />
'''Crystal Structure of Prolyl-tRNA Synthetase from Methanocaldococcus janaschii'''<br />


==Overview==
==Crystal Structure of Prolyl-tRNA Synthetase from Methanocaldococcus janaschii==
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.
<StructureSection load='1nj8' size='340' side='right'caption='[[1nj8]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nj8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NJ8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nj8 OCA], [https://pdbe.org/1nj8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nj8 RCSB], [https://www.ebi.ac.uk/pdbsum/1nj8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nj8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYP_METJA SYP_METJA] Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process non-cognate amino acids such as cysteine and alanine.<ref>PMID:10642548</ref> <ref>PMID:10869184</ref> <ref>PMID:11141055</ref> <ref>PMID:11866507</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nj/1nj8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nj8 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1NJ8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NJ8 OCA].
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
== References ==
==Reference==
<references/>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12578991 12578991]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Proline--tRNA ligase]]
[[Category: Kamtekar S]]
[[Category: Single protein]]
[[Category: Kennedy WD]]
[[Category: Kamtekar, S.]]
[[Category: Soll D]]
[[Category: Kennedy, W.D.]]
[[Category: Stathopoulos C]]
[[Category: Soll, D.]]
[[Category: Steitz TA]]
[[Category: Stathopoulos, C.]]
[[Category: Wang J]]
[[Category: Steitz, T.A.]]
[[Category: Wang, J.]]
[[Category: class-ii trna synthetase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:18:52 2007''

Latest revision as of 07:57, 14 February 2024

Crystal Structure of Prolyl-tRNA Synthetase from Methanocaldococcus janaschii

1nj8, resolution 3.20Å

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