This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1t0k

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1t0k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0k, resolution 3.24&Aring;" /> '''Joint X-ray and NMR ...)
Line 1: Line 1:
-
[[Image:1t0k.gif|left|200px]]<br /><applet load="1t0k" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1t0k.gif|left|200px]]<br /><applet load="1t0k" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1t0k, resolution 3.24&Aring;" />
caption="1t0k, resolution 3.24&Aring;" />
'''Joint X-ray and NMR Refinement of Yeast L30e-mRNA complex'''<br />
'''Joint X-ray and NMR Refinement of Yeast L30e-mRNA complex'''<br />
==Overview==
==Overview==
-
L30e, a Saccharomyces cervisiae ribosomal protein, regulates its own, expression by binding to a purine-rich asymmetric internal loop located in, both its pre-mRNA and mature mRNA. A crystal structure of an MBP-L30e, fusion protein in complex with an RNA containing the pre-mRNA regulatory, site was solved at 3.24 A. Interestingly, the structure of the RNA, differed from that observed in a previously determined NMR structure of, the complex. Analysis of the NMR data led to the identification of a, single imino proton resonance in the internal loop that had been, incorrectly assigned and was principally responsible for the erroneous RNA, structure. A structure refinement was performed using both the X-ray, diffraction data and the NMR-derived distance and angle restraints. The, joint NMR and X-ray refinement resulted in improved stereochemistry and, lower crystallographic R factors. The RNA internal loop of the, MBP-L30e-mRNA complex adopts the canonical K-turn fold.
+
L30e, a Saccharomyces cervisiae ribosomal protein, regulates its own expression by binding to a purine-rich asymmetric internal loop located in both its pre-mRNA and mature mRNA. A crystal structure of an MBP-L30e fusion protein in complex with an RNA containing the pre-mRNA regulatory site was solved at 3.24 A. Interestingly, the structure of the RNA differed from that observed in a previously determined NMR structure of the complex. Analysis of the NMR data led to the identification of a single imino proton resonance in the internal loop that had been incorrectly assigned and was principally responsible for the erroneous RNA structure. A structure refinement was performed using both the X-ray diffraction data and the NMR-derived distance and angle restraints. The joint NMR and X-ray refinement resulted in improved stereochemistry and lower crystallographic R factors. The RNA internal loop of the MBP-L30e-mRNA complex adopts the canonical K-turn fold.
==About this Structure==
==About this Structure==
-
1T0K is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MTT as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entries 1CK5, 1CK8, 1CN8 and 1CN9. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T0K OCA].
+
1T0K is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MTT:'>MTT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entries 1CK5, 1CK8, 1CN8 and 1CN9. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0K OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Chao, J.A.]]
+
[[Category: Chao, J A.]]
-
[[Category: Williamson, J.R.]]
+
[[Category: Williamson, J R.]]
[[Category: MTT]]
[[Category: MTT]]
[[Category: joint nmr and x-ray refinement]]
[[Category: joint nmr and x-ray refinement]]
Line 21: Line 21:
[[Category: ribosomal protein l30e]]
[[Category: ribosomal protein l30e]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:53:51 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:35 2008''

Revision as of 13:08, 21 February 2008


1t0k, resolution 3.24Å

Drag the structure with the mouse to rotate

Joint X-ray and NMR Refinement of Yeast L30e-mRNA complex

Overview

L30e, a Saccharomyces cervisiae ribosomal protein, regulates its own expression by binding to a purine-rich asymmetric internal loop located in both its pre-mRNA and mature mRNA. A crystal structure of an MBP-L30e fusion protein in complex with an RNA containing the pre-mRNA regulatory site was solved at 3.24 A. Interestingly, the structure of the RNA differed from that observed in a previously determined NMR structure of the complex. Analysis of the NMR data led to the identification of a single imino proton resonance in the internal loop that had been incorrectly assigned and was principally responsible for the erroneous RNA structure. A structure refinement was performed using both the X-ray diffraction data and the NMR-derived distance and angle restraints. The joint NMR and X-ray refinement resulted in improved stereochemistry and lower crystallographic R factors. The RNA internal loop of the MBP-L30e-mRNA complex adopts the canonical K-turn fold.

About this Structure

1T0K is a Protein complex structure of sequences from Escherichia coli and Saccharomyces cerevisiae with as ligand. This structure supersedes the now removed PDB entries 1CK5, 1CK8, 1CN8 and 1CN9. Full crystallographic information is available from OCA.

Reference

Joint X-ray and NMR refinement of the yeast L30e-mRNA complex., Chao JA, Williamson JR, Structure. 2004 Jul;12(7):1165-76. PMID:15242593

Page seeded by OCA on Thu Feb 21 15:08:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools