1ha3: Difference between revisions

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Revision as of 12:34, 20 March 2008

File:1ha3.gif

, resolution 2.00Å

Sites:

, , , , and

Ligands:

, , and

Gene:

TUFB (Thermus aquaticus)

Activity:

dGTPase, with EC number 3.1.5.1

Coordinates:

save as pdb, mmCIF, xml

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. 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

Page seeded by OCA on Thu Mar 20 11:34:21 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ha3.gif|left|200px]]<br /><applet load="1ha3" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ha3.gif|left|200px]]
-caption="1ha3, resolution 2.00&Aring;" />
-'''ELONGATION FACTOR TU IN COMPLEX WITH AURODOX'''<br />
+ {{Structure
+|PDB= 1ha3 |SIZE=350|CAPTION= <scene name='initialview01'>1ha3</scene>, resolution 2.00&Aring;
+|SITE= <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>
+|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MAU:N-METHYL+KIRROMYCIN'>MAU</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
+|ACTIVITY= [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]
+|GENE= TUFB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 Thermus aquaticus])
+}}
+'''ELONGATION FACTOR TU IN COMPLEX WITH AURODOX'''
 ==Overview==
@@ Line 7: / Line 16: @@
 ==About this Structure==
-HA3 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].
+HA3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HA3 OCA].
 ==Reference==
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11278992 11278992]
+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:[http://www.ncbi.nlm.nih.gov/pubmed/11278992 11278992]
 [[Category: Single protein]]
 [[Category: Thermus aquaticus]]
@@ Line 28: / Line 37: @@
 [[Category: ribosome]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:34:21 2008''