3eza
From Proteopedia
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| - | [[Image:3eza.jpg|left|200px]] | + | [[Image:3eza.jpg|left|200px]] |
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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''' | + | {{Structure |
| + | |PDB= 3eza |SIZE=350|CAPTION= <scene name='initialview01'>3eza</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3EZA is a [ | + | 3EZA is a [[Protein complex]] structure of sequences 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=3EZA OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10048929 10048929] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Phosphoenolpyruvate--protein phosphotransferase]] | [[Category: Phosphoenolpyruvate--protein phosphotransferase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 19:04:40 2008'' |
Revision as of 17:04, 20 March 2008
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| Activity: | Phosphoenolpyruvate--protein phosphotransferase, with EC number 2.7.3.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE
Overview
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
3EZA is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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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