We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1q99

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1q99.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1q99.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q99| PDB=1q99 | SCENE= }}
{{STRUCTURE_1q99| PDB=1q99 | SCENE= }}
-
'''Crystal structure of the Saccharomyces cerevisiae SR protein kinsae, Sky1p, complexed with the non-hydrolyzable ATP analogue, AMP-PNP'''
+
===Crystal structure of the Saccharomyces cerevisiae SR protein kinsae, Sky1p, complexed with the non-hydrolyzable ATP analogue, AMP-PNP===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12911299}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12911299 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12911299}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Vu, D.]]
[[Category: Vu, D.]]
[[Category: Protein kinase]]
[[Category: Protein kinase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:01:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:05:04 2008''

Revision as of 20:05, 27 July 2008

Image:1q99.png

Template:STRUCTURE 1q99

Crystal structure of the Saccharomyces cerevisiae SR protein kinsae, Sky1p, complexed with the non-hydrolyzable ATP analogue, AMP-PNP

Template:ABSTRACT PUBMED 12911299

About this Structure

1Q99 is a Single protein structure of sequence from Saccharomyces cerevisiae. 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 Sun Jul 27 23:05:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q99"
Personal tools