1q97: Difference between revisions

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New page: left|200px<br /><applet load="1q97" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q97, resolution 2.30Å" /> '''The structure of the...
 
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[[Image:1q97.gif|left|200px]]<br /><applet load="1q97" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1q97, resolution 2.30&Aring;" />
'''The structure of the Saccharomyces cerevisiae SR protein kinase, Sky1p, with bound ATP'''<br />


==Overview==
==The structure of the Saccharomyces cerevisiae SR protein kinase, Sky1p, with bound ATP==
Conformational changes are thought to play a key role in the function of, active protein kinases, although little is known about how these changes, relate to the mechanism of phosphorylation. Here we present four, high-resolution structures of a single crystal form of Sky1p, a, constitutively active serine kinase implicated in yeast RNA processing, each in a different state of nucleotide binding. By comparing the, apoenzyme structure to the ADP- and ATP-bound Sky1p structures, we have, revealed conformational changes caused by ATP binding or conversion from, nucleotide reactant to product. Rotation of the small lobe of the kinase, closes the cleft upon binding, allowing the nucleotide to interact with, residues from both lobes of the kinase, although some interactions thought, to be important for phosphotransfer are missing in the ATP-containing, structure. In the apoenzyme, a kinase-conserved phosphate-anchoring loop, is in a twisted conformation that is incompatible with ADP and ATP, binding, providing a potential mechanism for facilitating ADP release in, Sky1p. The nonhydrolyzable ATP analogue AMP-PNP binds in a unique mode, that fails to induce lobe closure. This observation, along with, comparisons between the two independent molecules in the asymmetric unit, of each structure, has provided new molecular details about how the, nucleotide binds and induces closure. Finally, we have used mutational, analysis to establish the importance of a glycine within the linker that, connects the two lobes of Sky1p.
<StructureSection load='1q97' size='340' side='right'caption='[[1q97]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1q97]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q97 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1q97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q97 OCA], [https://pdbe.org/1q97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q97 RCSB], [https://www.ebi.ac.uk/pdbsum/1q97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q97 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SKY1_YEAST SKY1_YEAST] Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.<ref>PMID:11175909</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/q9/1q97_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=1q97 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1Q97 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG, NI, SO4, ATP and ADN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q97 OCA].
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
 
== References ==
==Reference==
<references/>
Nucleotide-induced conformational changes in the Saccharomyces cerevisiae SR protein kinase, Sky1p, revealed by X-ray crystallography., Nolen B, Ngo J, Chakrabarti S, Vu D, Adams JA, Ghosh G, Biochemistry. 2003 Aug 19;42(32):9575-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12911299 12911299]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Adams JA]]
[[Category: Adams, J.A.]]
[[Category: Chakrabarti S]]
[[Category: Chakrabarti, S.]]
[[Category: Ghosh G]]
[[Category: Ghosh, G.]]
[[Category: Ngo J]]
[[Category: Ngo, J.]]
[[Category: Nolen B]]
[[Category: Nolen, B.]]
[[Category: Vu D]]
[[Category: Vu, D.]]
[[Category: ADN]]
[[Category: ATP]]
[[Category: MG]]
[[Category: NI]]
[[Category: SO4]]
[[Category: protein kinase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:30:06 2007''

Latest revision as of 11:13, 14 February 2024

The structure of the Saccharomyces cerevisiae SR protein kinase, Sky1p, with bound ATPThe structure of the Saccharomyces cerevisiae SR protein kinase, Sky1p, with bound ATP

Structural highlights

1q97 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SKY1_YEAST Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Nolen B, Yun CY, Wong CF, McCammon JA, Fu XD, Ghosh G. The structure of Sky1p reveals a novel mechanism for constitutive activity. Nat Struct Biol. 2001 Feb;8(2):176-83. PMID:11175909 doi:10.1038/84178

1q97, resolution 2.30Å

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