Phosphotransferase

From Proteopedia

Revision as of 12:42, 28 August 2016

spinqualitylabelsall models Aminoglycoside phosphotransferase complex with gentamycin, and glycerol (PDB entry 3ham) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Phosphotransferase (PT) are enzymes which catalyze phosphorylation reactions. The acceptor group can be alcohol, carboxy, nitrogenous, phosphate or a pair ofd groups. Aminoglycoside PT (AGPT) inactivate aminoglycoside antibiotics by phosphorylation[1]. Phosphoenolpyruvate-protein PT (PEP) catalyzes the phosphorylation of protein histidine residues[2]. Sporulation initiation PT (Spo0B, Spo0F) are elements in the phosphorelay system which regulates the initiation of sporulation[3]. See: Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System Enzyme I of the S. aureus PTS User:Karl Oberholser/Phosphoenolpyruvate:Sugar Phosphotransferase for a flash movie. Structural highlights The is located at a structural cleft and contains the [4]. Water molecules shown as red spheres.

3D structures of phosphotransferase

Updated on 28-August-2016

References

1. ↑ Wright GD, Thompson PR. Aminoglycoside phosphotransferases: proteins, structure, and mechanism. Front Biosci. 1999 Jan 1;4:D9-21. PMID:9872733
2. ↑ Mizrachi Nebenzahl Y, Blau K, Kushnir T, Shagan M, Portnoi M, Cohen A, Azriel S, Malka I, Adawi A, Kafka D, Dotan S, Guterman G, Troib S, Fishilevich T, Gershoni JM, Braiman A, Mitchell AM, Mitchell TJ, Porat N, Goliand I, Chalifa Caspi V, Swiatlo E, Tal M, Ellis R, Elia N, Dagan R. Streptococcus pneumoniae Cell-Wall-Localized Phosphoenolpyruvate Protein Phosphotransferase Can Function as an Adhesin: Identification of Its Host Target Molecules and Evaluation of Its Potential as a Vaccine. PLoS One. 2016 Mar 18;11(3):e0150320. doi: 10.1371/journal.pone.0150320., eCollection 2016. PMID:26990554 doi:http://dx.doi.org/10.1371/journal.pone.0150320
3. ↑ Trach K, Burbulys D, Strauch M, Wu JJ, Dhillon N, Jonas R, Hanstein C, Kallio P, Perego M, Bird T, et al.. Control of the initiation of sporulation in Bacillus subtilis by a phosphorelay. Res Microbiol. 1991 Sep-Oct;142(7-8):815-23. PMID:1664534
4. ↑ Young PG, Walanj R, Lakshmi V, Byrnes LJ, Metcalf P, Baker EN, Vakulenko SB, Smith CA. The crystal structures of substrate and nucleotide complexes of Enterococcus faecium aminoglycoside-2-phosphotransferase-IIa [APH(2)-IIa] provide insights into substrate selectivity in the APH(2) subfamily. J Bacteriol. 2009 Jul;191(13):4133-43. Epub 2009 May 8. PMID:19429619 doi:10.1128/JB.00149-09