1gh8: Difference between revisions
New page: left|200px<br /><applet load="1gh8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gh8" /> '''SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATI... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1gh8.gif|left|200px]]<br /><applet load="1gh8" size=" | [[Image:1gh8.gif|left|200px]]<br /><applet load="1gh8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1gh8" /> | caption="1gh8" /> | ||
'''SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br /> | '''SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br /> | ||
==Overview== | ==Overview== | ||
The tertiary fold of the elongation factor, aEF-1beta, from | The tertiary fold of the elongation factor, aEF-1beta, from Methanobacterium thermoautotrophicum was determined in a high-throughput fashion using a minimal set of NMR experiments. NMR secondary structure prediction, deuterium exchange experiments and the analysis of chemical shift perturbations were combined to identify the protein fold as an alpha-beta sandwich typical of many RNA binding proteins including EF-G. Following resolution of the tertiary fold, a high resolution structure of aEF-1beta was determined using heteronuclear and homonuclear NMR experiments and a semi-automated NOESY assignment strategy. Analysis of the aEF-1beta structure revealed close similarity to its human analogue, eEF-1beta. In agreement with studies on EF-Ts and human EF-1beta, a functional mechanism for nucleotide exchange is proposed wherein Phe46 on an exposed loop acts as a lever to eject GDP from the associated elongation factor G-protein, aEF-1alpha. aEF-1beta was also found to bind calcium in the groove between helix alpha2 and strand beta4. This novel feature was not observed previously and may serve a structural function related to protein stability or may play a functional role in archaeal protein translation. | ||
==About this Structure== | ==About this Structure== | ||
1GH8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. This structure | 1GH8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. This structure supersedes the now removed PDB entry 1D5K. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GH8 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 16: | Line 16: | ||
[[Category: Gehring, K.]] | [[Category: Gehring, K.]] | ||
[[Category: Kozlov, G.]] | [[Category: Kozlov, G.]] | ||
[[Category: NESG, Northeast | [[Category: NESG, Northeast Structural Genomics Consortium.]] | ||
[[Category: alpha-beta sandwich]] | [[Category: alpha-beta sandwich]] | ||
[[Category: gene regulation]] | [[Category: gene regulation]] | ||
| Line 25: | Line 25: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:59 2008'' | ||
Revision as of 13:50, 21 February 2008
|
SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
OverviewOverview
The tertiary fold of the elongation factor, aEF-1beta, from Methanobacterium thermoautotrophicum was determined in a high-throughput fashion using a minimal set of NMR experiments. NMR secondary structure prediction, deuterium exchange experiments and the analysis of chemical shift perturbations were combined to identify the protein fold as an alpha-beta sandwich typical of many RNA binding proteins including EF-G. Following resolution of the tertiary fold, a high resolution structure of aEF-1beta was determined using heteronuclear and homonuclear NMR experiments and a semi-automated NOESY assignment strategy. Analysis of the aEF-1beta structure revealed close similarity to its human analogue, eEF-1beta. In agreement with studies on EF-Ts and human EF-1beta, a functional mechanism for nucleotide exchange is proposed wherein Phe46 on an exposed loop acts as a lever to eject GDP from the associated elongation factor G-protein, aEF-1alpha. aEF-1beta was also found to bind calcium in the groove between helix alpha2 and strand beta4. This novel feature was not observed previously and may serve a structural function related to protein stability or may play a functional role in archaeal protein translation.
About this StructureAbout this Structure
1GH8 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. This structure supersedes the now removed PDB entry 1D5K. Full crystallographic information is available from OCA.
ReferenceReference
Rapid fold and structure determination of the archaeal translation elongation factor 1beta from Methanobacterium thermoautotrophicum., Kozlov G, Ekiel I, Beglova N, Yee A, Dharamsi A, Engel A, Siddiqui N, Nong A, Gehring K, J Biomol NMR. 2000 Jul;17(3):187-94. PMID:10959626
Page seeded by OCA on Thu Feb 21 12:49:59 2008