1q97
From Proteopedia
(New page: 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=" | + | [[Image:1q97.gif|left|200px]]<br /><applet load="1q97" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q97, resolution 2.30Å" /> | caption="1q97, resolution 2.30Å" /> | ||
'''The structure of the Saccharomyces cerevisiae SR protein kinase, Sky1p, with bound ATP'''<br /> | '''The structure of the Saccharomyces cerevisiae SR protein kinase, Sky1p, with bound ATP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Conformational changes are thought to play a key role in the function of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=ADN:'>ADN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q97 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Adams, J | + | [[Category: Adams, J A.]] |
[[Category: Chakrabarti, S.]] | [[Category: Chakrabarti, S.]] | ||
[[Category: Ghosh, G.]] | [[Category: Ghosh, G.]] | ||
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[[Category: protein kinase]] | [[Category: protein kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:12 2008'' |
Revision as of 12:37, 21 February 2008
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The structure of the Saccharomyces cerevisiae SR protein kinase, Sky1p, with bound ATP
Overview
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.
About this Structure
1Q97 is a Single protein structure of sequence from Saccharomyces cerevisiae with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
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:12911299
Page seeded by OCA on Thu Feb 21 14:37:12 2008
Categories: Saccharomyces cerevisiae | Single protein | Adams, J A. | Chakrabarti, S. | Ghosh, G. | Ngo, J. | Nolen, B. | Vu, D. | ADN | ATP | MG | NI | SO4 | Protein kinase
