3eze: Difference between revisions
New page: left|200px<br /><applet load="3eze" size="450" color="white" frame="true" align="right" spinBox="true" caption="3eze" /> '''COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZY... |
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'''COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE'''<br /> | '''COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
The solution structure of the first protein-protein complex of the | The solution structure of the first protein-protein complex of the bacterial phosphoenolpyruvate: sugar phosphotransferase system between the N-terminal domain of enzyme I (EIN) and the histidine-containing phosphocarrier protein HPr has been determined by NMR spectroscopy, including the use of residual dipolar couplings that provide long-range structural information. The complex between EIN and HPr is a classical example of surface complementarity, involving an essentially all helical interface, comprising helices 2, 2', 3 and 4 of the alpha-subdomain of EIN and helices 1 and 2 of HPr, that requires virtually no changes in conformation of the components relative to that in their respective free states. The specificity of the complex is dependent on the correct placement of both van der Waals and electrostatic contacts. The transition state can be formed with minimal changes in overall conformation, and is stabilized in favor of phosphorylated HPr, thereby accounting for the directionality of phosphoryl transfer. | ||
==About this Structure== | ==About this Structure== | ||
3EZE 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 PO3 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoenolpyruvate--protein_phosphotransferase Phosphoenolpyruvate--protein phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.9 2.7.3.9] Full crystallographic information is available from [http:// | 3EZE 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=PO3:'>PO3</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoenolpyruvate--protein_phosphotransferase Phosphoenolpyruvate--protein phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.9 2.7.3.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EZE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Phosphoenolpyruvate--protein phosphotransferase]] | [[Category: Phosphoenolpyruvate--protein phosphotransferase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Clore, G | [[Category: Clore, G M.]] | ||
[[Category: Garrett, D | [[Category: Garrett, D S.]] | ||
[[Category: Gronenborn, A | [[Category: Gronenborn, A M.]] | ||
[[Category: PO3]] | [[Category: PO3]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
| Line 23: | Line 23: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:27 2008'' | ||
Revision as of 20:09, 21 February 2008
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COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE
OverviewOverview
The solution structure of the first protein-protein complex of the bacterial phosphoenolpyruvate: sugar phosphotransferase system between the N-terminal domain of enzyme I (EIN) and the histidine-containing phosphocarrier protein HPr has been determined by NMR spectroscopy, including the use of residual dipolar couplings that provide long-range structural information. The complex between EIN and HPr is a classical example of surface complementarity, involving an essentially all helical interface, comprising helices 2, 2', 3 and 4 of the alpha-subdomain of EIN and helices 1 and 2 of HPr, that requires virtually no changes in conformation of the components relative to that in their respective free states. The specificity of the complex is dependent on the correct placement of both van der Waals and electrostatic contacts. The transition state can be formed with minimal changes in overall conformation, and is stabilized in favor of phosphorylated HPr, thereby accounting for the directionality of phosphoryl transfer.
About this StructureAbout this Structure
3EZE is a Protein complex structure of sequences from Escherichia coli with as ligand. Active as Phosphoenolpyruvate--protein phosphotransferase, with EC number 2.7.3.9 Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr., Garrett DS, Seok YJ, Peterkofsky A, Gronenborn AM, Clore GM, Nat Struct Biol. 1999 Feb;6(2):166-73. PMID:10048929
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