Phosphotransferase
From Proteopedia
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| - | + | <StructureSection load='3ham' size='350' side='right' caption='Aminoglycoside phosphotransferase complex with gentamycin, and glycerol (PDB entry [[3ham]])' scene=''> | |
| + | == Function == | ||
'''Phosphotransferase''' (PT) are enzymes which catalyze phosphorylation reactions. The acceptor group can be alcohol, carboxy, nitrogenous, phosphate or a pair ofd groups.<br /> | '''Phosphotransferase''' (PT) are enzymes which catalyze phosphorylation reactions. The acceptor group can be alcohol, carboxy, nitrogenous, phosphate or a pair ofd groups.<br /> | ||
* '''Aminoglycoside PT''' (AGPT) inactivate aminoglycoside antibiotics by phosphorylation<ref>PMID:9872733</ref>.<br /> | * '''Aminoglycoside PT''' (AGPT) inactivate aminoglycoside antibiotics by phosphorylation<ref>PMID:9872733</ref>.<br /> | ||
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* [[Enzyme I of the S. aureus PTS]]<br /> | * [[Enzyme I of the S. aureus PTS]]<br /> | ||
* [[User:Karl Oberholser/Phosphoenolpyruvate:Sugar Phosphotransferase]] for a flash movie. | * [[User:Karl Oberholser/Phosphoenolpyruvate:Sugar Phosphotransferase]] for a flash movie. | ||
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| + | == Structural highlights == | ||
| + | The active site of amino glycoside PT is located at a structural cleft and contains the aspartate catalytic base<ref>PMID:19429619</ref>. | ||
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| + | </StructureSection> | ||
==3D structures of phosphotransferase== | ==3D structures of phosphotransferase== | ||
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*Aminoglycoside phosphotransferase complex with antibiotic | *Aminoglycoside phosphotransferase complex with antibiotic | ||
| - | **[[ | + | **[[3ham]] - EfAGPT + antibiotic <BR /> |
| + | **[[3hav]] - EfAGPT + ATP + antibiotic <BR /> | ||
**[[3h8p]], [[3tm0]] - EfAGPT + AMP-PNP + antibiotic<br /> | **[[3h8p]], [[3tm0]] - EfAGPT + AMP-PNP + antibiotic<br /> | ||
**[[2b0q]], [[1l8t]] - EfAGPT IIIA + ADP + antibiotic<br /> | **[[2b0q]], [[1l8t]] - EfAGPT IIIA + ADP + antibiotic<br /> | ||
Revision as of 09:40, 3 July 2016
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3D structures of phosphotransferase
Updated on 03-July-2016
References
- ↑ Wright GD, Thompson PR. Aminoglycoside phosphotransferases: proteins, structure, and mechanism. Front Biosci. 1999 Jan 1;4:D9-21. PMID:9872733
- ↑ 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
- ↑ 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
- ↑ 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
