1e0h: Difference between revisions
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'''INHIBITOR PROTEIN IM9 BOUND TO ITS PARTNER E9 DNASE''' | {{Structure | ||
|PDB= 1e0h |SIZE=350|CAPTION= <scene name='initialview01'>1e0h</scene> | |||
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|LIGAND= | |||
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'''INHIBITOR PROTEIN IM9 BOUND TO ITS PARTNER E9 DNASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E0H is a [ | 1E0H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0H OCA]. | ||
==Reference== | ==Reference== | ||
NMR investigation of the interaction of the inhibitor protein Im9 with its partner DNase., Boetzel R, Czisch M, Kaptein R, Hemmings AM, James R, Kleanthous C, Moore GR, Protein Sci. 2000 Sep;9(9):1709-18. PMID:[http:// | NMR investigation of the interaction of the inhibitor protein Im9 with its partner DNase., Boetzel R, Czisch M, Kaptein R, Hemmings AM, James R, Kleanthous C, Moore GR, Protein Sci. 2000 Sep;9(9):1709-18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11045617 11045617] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Moore, G R.]] | [[Category: Moore, G R.]] | ||
[[Category: colicin immunity protein]] | [[Category: colicin immunity protein]] | ||
[[Category: e-type | [[Category: e-type colicin]] | ||
[[Category: inhibitor of e9 dnase]] | [[Category: inhibitor of e9 dnase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:47:28 2008'' | ||
Revision as of 11:47, 20 March 2008
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INHIBITOR PROTEIN IM9 BOUND TO ITS PARTNER E9 DNASE
OverviewOverview
The bacterial toxin colicin E9 is secreted by producing Escherichia coli cells with its 9.5 kDa inhibitor protein Im9 bound tightly to its 14.5 kDa C-terminal DNase domain. Double- and triple-resonance NMR spectra of the 24 kDa complex of uniformly 13C and 15N labeled Im9 bound to the unlabeled DNase domain have provided sufficient constraints for the solution structure of the bound Im9 to be determined. For the final ensemble of 20 structures, pairwise RMSDs for residues 3-84 were 0.76 +/- 0.14 A for the backbone atoms and 1.36 +/- 0.15 A for the heavy atoms. Representative solution structures of the free and bound Im9 are highly similar, with backbone and heavy atom RMSDs of 1.63 and 2.44 A, respectively, for residues 4-83, suggesting that binding does not cause a major conformational change in Im9. The NMR studies have also allowed the DNase contact surface on Im9 to be investigated through changes in backbone chemical shifts and NOEs between the two proteins determined from comparisons of 1H-1H-13C NOESY-HSQC spectra with and without 13C decoupling. The NMR-defined interface agrees well with that determined in a recent X-ray structure analysis with the major difference being that a surface loop of Im9, which is at the interface, has a different conformation in the solution and crystal structures. Tyr54, a key residue on the interface, is shown to exhibit NMR characteristics indicative of slow rotational flipping. A mechanistic description of the influence binding of Im9 has on the dynamic behavior of E9 DNase, which is known to exist in two slowly interchanging conformers in solution, is proposed.
About this StructureAbout this Structure
1E0H is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
NMR investigation of the interaction of the inhibitor protein Im9 with its partner DNase., Boetzel R, Czisch M, Kaptein R, Hemmings AM, James R, Kleanthous C, Moore GR, Protein Sci. 2000 Sep;9(9):1709-18. PMID:11045617
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