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2hcj

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[[Image:2hcj.jpg|left|200px]]
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{{STRUCTURE_2hcj| PDB=2hcj | SCENE= }}
{{STRUCTURE_2hcj| PDB=2hcj | SCENE= }}
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'''"Trypsin-modified Elongation Factor Tu in complex with tetracycline"'''
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==="Trypsin-modified Elongation Factor Tu in complex with tetracycline"===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17057344 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17057344}}
==About this Structure==
==About this Structure==
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[[Category: Gtpase center]]
[[Category: Gtpase center]]
[[Category: Trypsin-modified ef-tu]]
[[Category: Trypsin-modified ef-tu]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:07:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:55:59 2008''

Revision as of 16:56, 28 July 2008

Image:2hcj.png

Template:STRUCTURE 2hcj

"Trypsin-modified Elongation Factor Tu in complex with tetracycline"

Template:ABSTRACT PUBMED 17057344

About this Structure

2HCJ is a Protein complex structure of sequences from Escherichia coli. 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 Mon Jul 28 19:55:59 2008

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