2f3g
From Proteopedia
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|SITE= <scene name='pdbsite=AVE:Molecule+Is+Transiently+Phosphorylated+At+HIS+90'>AVE</scene> | |SITE= <scene name='pdbsite=AVE:Molecule+Is+Transiently+Phosphorylated+At+HIS+90'>AVE</scene> | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f3g OCA], [http://www.ebi.ac.uk/pdbsum/2f3g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f3g RCSB]</span> | ||
}} | }} | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:57:24 2008'' |
Revision as of 23:57, 30 March 2008
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| , resolution 2.13Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Activity: | Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
IIAGLC CRYSTAL FORM III
Overview
In Escherichia coli, the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS), IIAGlc (IIIGlc in older literature), is also the central regulatory protein of the PTS. Depending upon its state of phosphorylation, IIAGlc binds to a number of different proteins that display no apparent sequence homology. Previous structural studies suggested that nonspecific hydrophobic interactions, specific salt bridges, and an intermolecular Zn(II) binding site contribute to the wide latitude in IIAGlc binding sites. Two new crystal forms of IIAGlc have been solved at high resolution, and the models were compared to those previously studied. The major intermolecular contacts in the crystals differ in detail, but all involve the hydrophobic active site of IIAGlc interacting with a hydrophobic patch on a neighbor and all are shown to be surprisingly similar to the physiologically relevant regulatory interaction of IIAGlc with glycerol kinase. In two crystal forms, a helix on one molecule interacts with the face of another, while in the other crystal form, the primary crystal contact consists of a strand of beta-sheet that contributes to an intermolecular Zn(II) binding site with tetrahedral ligation identical to that of the zinc peptidase thermolysin. Thus, relatively nonspecific hydrophobic interactions combined with specific salt bridges and an intermolecular cation binding site (cation-promoted association) permit a regulatory protein to bind to target proteins that have little or no sequence or structural homology with one another. It is suggested that signal transduction by IIAGlc is a binary switch in which phosphorylation at the active site directly controls binding to target molecules.
About this Structure
2F3G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural studies of the Escherichia coli signal transducing protein IIAGlc: implications for target recognition., Feese MD, Comolli L, Meadow ND, Roseman S, Remington SJ, Biochemistry. 1997 Dec 23;36(51):16087-96. PMID:9405042
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