2hcj
From Proteopedia
(New page: 200px<br /><applet load="2hcj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hcj, resolution 2.12Å" /> '''"Trypsin-modified El...) |
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| - | [[Image:2hcj.jpg|left|200px]]<br /><applet load="2hcj" size=" | + | [[Image:2hcj.jpg|left|200px]]<br /><applet load="2hcj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hcj, resolution 2.12Å" /> | caption="2hcj, resolution 2.12Å" /> | ||
'''"Trypsin-modified Elongation Factor Tu in complex with tetracycline"'''<br /> | '''"Trypsin-modified Elongation Factor Tu in complex with tetracycline"'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two crystal forms of a complex between trypsin-modified elongation factor | + | Two crystal forms of a complex between trypsin-modified elongation factor Tu-MgGDP from Escherichia coli and the antibiotic tetracycline have been solved by X-ray diffraction analysis to resolutions of 2.8 and 2.1 A, respectively. In the P2(1) form, cocrystals were grown from a solution mixture of the protein and tetracycline. Six copies of the trypsin-modified EF-Tu-MgGDP-tetracycline complex are arranged as three sets of dimers in the asymmetric unit. In the second crystal form, tetracycline was diffused into P4(3)2(1)2 crystals, resulting in a monomeric complex in the asymmetric unit. Atomic coordinates have been refined to crystallographic R factors of 18.0% for the P2(1) form and 20.0% for the P4(3)2(1)2 form. In both complexes, tetracycline makes significant interactions with the GTPase active site of EF-Tu. The phenoldiketone moiety of tetracycline interacts directly with the Mg(2+), the alpha-phosphate group of GDP and two amino acids, Thr25 and Asp80, which are conserved in the GX(4)GKS/T and DX(2)G sequence motifs found in all GTPases and many ATPases. The molecular complementarity, previously unrecognized between invariant groups present in all GTPase/ATPases and the active moiety of tetracycline, may have wide-ranging implications for all drugs containing the phenoldiketone moiety as well as for the design of new compounds targeted against a broad range of GTPases or ATPases. |
==About this Structure== | ==About this Structure== | ||
| - | 2HCJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, NA, SO4, TAC, GDP and GLV as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2HCJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=TAC:'>TAC</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=GLV:'>GLV</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HCJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Aorora, A.]] | [[Category: Aorora, A.]] | ||
[[Category: Bergmann, E.]] | [[Category: Bergmann, E.]] | ||
| - | [[Category: Heffron, S | + | [[Category: Heffron, S E.]] |
[[Category: Jurnak, F.]] | [[Category: Jurnak, F.]] | ||
[[Category: Mui, S.]] | [[Category: Mui, S.]] | ||
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[[Category: trypsin-modified ef-tu]] | [[Category: trypsin-modified ef-tu]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:40:32 2008'' |
Revision as of 15:40, 21 February 2008
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"Trypsin-modified Elongation Factor Tu in complex with tetracycline"
Overview
Two crystal forms of a complex between trypsin-modified elongation factor Tu-MgGDP from Escherichia coli and the antibiotic tetracycline have been solved by X-ray diffraction analysis to resolutions of 2.8 and 2.1 A, respectively. In the P2(1) form, cocrystals were grown from a solution mixture of the protein and tetracycline. Six copies of the trypsin-modified EF-Tu-MgGDP-tetracycline complex are arranged as three sets of dimers in the asymmetric unit. In the second crystal form, tetracycline was diffused into P4(3)2(1)2 crystals, resulting in a monomeric complex in the asymmetric unit. Atomic coordinates have been refined to crystallographic R factors of 18.0% for the P2(1) form and 20.0% for the P4(3)2(1)2 form. In both complexes, tetracycline makes significant interactions with the GTPase active site of EF-Tu. The phenoldiketone moiety of tetracycline interacts directly with the Mg(2+), the alpha-phosphate group of GDP and two amino acids, Thr25 and Asp80, which are conserved in the GX(4)GKS/T and DX(2)G sequence motifs found in all GTPases and many ATPases. The molecular complementarity, previously unrecognized between invariant groups present in all GTPase/ATPases and the active moiety of tetracycline, may have wide-ranging implications for all drugs containing the phenoldiketone moiety as well as for the design of new compounds targeted against a broad range of GTPases or ATPases.
About this Structure
2HCJ is a Protein complex structure of sequences from Escherichia coli with , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Molecular complementarity between tetracycline and the GTPase active site of elongation factor Tu., Heffron SE, Mui S, Aorora A, Abel K, Bergmann E, Jurnak F, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1392-400. Epub, 2006 Oct 18. PMID:17057344
Page seeded by OCA on Thu Feb 21 17:40:32 2008
Categories: Escherichia coli | Protein complex | Abel, K. | Aorora, A. | Bergmann, E. | Heffron, S E. | Jurnak, F. | Mui, S. | GDP | GLV | MG | NA | SO4 | TAC | Complex with tetracycline | Gtpase center | Trypsin-modified ef-tu
