1ha3: Difference between revisions
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[[Image:1ha3.gif|left|200px]]<br /><applet load="1ha3" size=" | [[Image:1ha3.gif|left|200px]]<br /><applet load="1ha3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ha3, resolution 2.00Å" /> | caption="1ha3, resolution 2.00Å" /> | ||
'''ELONGATION FACTOR TU IN COMPLEX WITH AURODOX'''<br /> | '''ELONGATION FACTOR TU IN COMPLEX WITH AURODOX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1HA3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with MG, GDP, MAU and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dGTPase dGTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.5.1 3.1.5.1] Known structural/functional Sites: <scene name='pdbsite=GDA:Gdp Binding Site For Chain A'>GDA</scene>, <scene name='pdbsite=GDB:Gdp Binding Site For Chain B'>GDB</scene>, <scene name='pdbsite=MAA:Mau Binding Site For Chain A Symmetry Related Subunits C ...'>MAA</scene>, <scene name='pdbsite=MAB:Mau Binding Site For Chain B Symmetry Related Subunits C ...'>MAB</scene>, <scene name='pdbsite=MGA:Mg Binding Site For Chain A'>MGA</scene> and <scene name='pdbsite=MGB:Mg Binding Site For Chain B'>MGB</scene>. Full crystallographic information is available from [http:// | 1HA3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GDP:'>GDP</scene>, <scene name='pdbligand=MAU:'>MAU</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dGTPase dGTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.5.1 3.1.5.1] Known structural/functional Sites: <scene name='pdbsite=GDA:Gdp+Binding+Site+For+Chain+A'>GDA</scene>, <scene name='pdbsite=GDB:Gdp+Binding+Site+For+Chain+B'>GDB</scene>, <scene name='pdbsite=MAA:Mau+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+C+...'>MAA</scene>, <scene name='pdbsite=MAB:Mau+Binding+Site+For+Chain+B+Symmetry+Related+Subunits+C+...'>MAB</scene>, <scene name='pdbsite=MGA:Mg+Binding+Site+For+Chain+A'>MGA</scene> and <scene name='pdbsite=MGB:Mg+Binding+Site+For+Chain+B'>MGB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HA3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: ribosome]] | [[Category: ribosome]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:48:11 2008'' | ||
Revision as of 10:48, 3 February 2008
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ELONGATION FACTOR TU IN COMPLEX WITH AURODOX
OverviewOverview
Aurodox is a member of the family of kirromycin antibiotics, which inhibit, protein biosynthesis by binding to elongation factor Tu (EF-Tu). We have, determined the crystal structure of the 1:1:1 complex of Thermus, thermophilus EF-Tu with GDP and aurodox to 2.0-A resolution. During its, catalytic cycle, EF-Tu adopts two strikingly different conformations, depending on the nucleotide bound: the GDP form and the GTP form. In the, present structure, a GTP complex-like conformation of EF-Tu is observed, although GDP is bound to the nucleotide-binding site. This is consistent, with previous proposals that aurodox fixes EF-Tu on the ribosome by, locking it in its GTP form. Binding of EF-Tu.GDP to aminoacyl-tRNA and, mutually exclusive binding of kirromycin and elongation factor Ts to EF-Tu, can be explained on the basis of the structure. For many previously, observed mutations that provide resistance to kirromycin, it can now be, understood how they prevent interaction with the antibiotic. An unexpected, feature of the structure is the reorientation of the His-85 side chain, toward the nucleotide-binding site. We propose that this residue, stabilizes the transition state of GTP hydrolysis, explaining the, acceleration of the reaction by kirromycin-type antibiotics.
About this StructureAbout this Structure
1HA3 is a Single protein structure of sequence from Thermus aquaticus with , , and as ligands. Active as dGTPase, with EC number 3.1.5.1 Known structural/functional Sites: , , , , and . Full crystallographic information is available from OCA.
ReferenceReference
Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox., Vogeley L, Palm GJ, Mesters JR, Hilgenfeld R, J Biol Chem. 2001 May 18;276(20):17149-55. Epub 2001 Jan 30. PMID:11278992
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