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[[Image:1kmm.gif|left|200px]]<br /><applet load="1kmm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kmm, resolution 2.6&Aring;" />
'''HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE'''<br />


==Overview==
==HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE==
The crystal structure of an enzyme-substrate complex with histidyl-tRNA, synthetase from Escherichia coli, ATP, and the amino acid analog, histidinol is described and compared with the previously obtained, enzyme-product complex with histidyl-adenylate. An active site arginine, Arg-259, unique to all histidyl-tRNA synthetases, plays the role of the, catalytic magnesium ion seen in seryl-tRNA synthetase. When Arg-259 is, substituted with histidine, the apparent second order rate constant, (kcat/Km) for the pyrophosphate exchange reaction and the aminoacylation, reaction decreases 1,000-fold and 500-fold, respectively. Crystals soaked, with MnCl2 reveal the existence of two metal binding sites between beta-, and gamma-phosphates; these sites appear to stabilize the conformation of, the pyrophosphate. The use of both conserved metal ions and arginine in, phosphoryl transfer provides evidence of significant early functional, divergence of class II aminoacyl-tRNA synthetases.
<StructureSection load='1kmm' size='340' side='right'caption='[[1kmm]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kmm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KMM 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HAM:HISTIDYL-ADENOSINE+MONOPHOSPHATE'>HAM</scene></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=1kmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmm OCA], [https://pdbe.org/1kmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kmm RCSB], [https://www.ebi.ac.uk/pdbsum/1kmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kmm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYH_ECOLI SYH_ECOLI]
== 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/km/1kmm_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=1kmm ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1KMM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=HAM:'>HAM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histidine--tRNA_ligase Histidine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21] Known structural/functional Sites: <scene name='pdbsite=S1A:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1A</scene>, <scene name='pdbsite=S1B:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1B</scene>, <scene name='pdbsite=S1C:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1C</scene> and <scene name='pdbsite=S1D:HIS+And+Atp+Binding+Site,+Product+Of+First+Reaction+(Int+...'>S1D</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMM OCA].
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase., Arnez JG, Augustine JG, Moras D, Francklyn CS, Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7144-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9207058 9207058]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Histidine--tRNA ligase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Arnez JG]]
[[Category: Arnez, J.G.]]
[[Category: Francklyn CS]]
[[Category: Francklyn, C.S.]]
[[Category: Moras D]]
[[Category: Moras, D.]]
[[Category: HAM]]
[[Category: aminoacyl-trna synthase]]
[[Category: ligase]]
[[Category: synthetase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:52:55 2008''

Latest revision as of 10:26, 14 February 2024

HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATEHISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE

Structural highlights

1kmm is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SYH_ECOLI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1kmm, resolution 2.60Å

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