Phosphotransferase
From Proteopedia
(Difference between revisions)
| Line 15: | Line 15: | ||
== Structural highlights == | == Structural highlights == | ||
The <scene name='45/456502/Cv/4'>active site of amino glycoside PT</scene> is located at a structural cleft and contains the <scene name='45/456502/Cv/5'>aspartate catalytic base</scene><ref>PMID:19429619</ref>. Water molecules are shown as red spheres. | The <scene name='45/456502/Cv/4'>active site of amino glycoside PT</scene> is located at a structural cleft and contains the <scene name='45/456502/Cv/5'>aspartate catalytic base</scene><ref>PMID:19429619</ref>. Water molecules are shown as red spheres. | ||
| + | |||
| + | ==3D structures of phosphotransferase== | ||
| + | [[Phosphotransferase 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
| Line 25: | Line 28: | ||
*'''Phosphotransferase''' | *'''Phosphotransferase''' | ||
| + | **[[1fyn]] – PT fyn SH3 domain + polyproline peptide - human<br /> | ||
| + | **[[1c02]] - PT - yeast<br /> | ||
**[[3our]] – PT IIA + pyruvate decarboxylase – ''Vibrio vulnificus''<BR /> | **[[3our]] – PT IIA + pyruvate decarboxylase – ''Vibrio vulnificus''<BR /> | ||
**[[2l5h]], [[2kx9]] - EcPT I - ''Escherichia coli'' – NMR<BR /> | **[[2l5h]], [[2kx9]] - EcPT I - ''Escherichia coli'' – NMR<BR /> | ||
| Line 33: | Line 38: | ||
**[[3ipj]] – PT IIABC – ''Clostridium difficile''<BR /> | **[[3ipj]] – PT IIABC – ''Clostridium difficile''<BR /> | ||
**[[2f9h]] - EfPT IIA – ''Enterococcus faecalis''<BR /> | **[[2f9h]] - EfPT IIA – ''Enterococcus faecalis''<BR /> | ||
| - | **[[1c02]] - PT - yeast<br /> | ||
**[[3n9x]] – PT – ''Plasmodium berghei''<br /> | **[[3n9x]] – PT – ''Plasmodium berghei''<br /> | ||
| - | **[[1fyn]] – PT fyn SH3 domain + polyproline peptide - human<br /> | ||
**[[4qpk]] – BaPT – ''Brucella abortus''<br /> | **[[4qpk]] – BaPT – ''Brucella abortus''<br /> | ||
**[[4qpj]] – BaPT + CTRA<br /> | **[[4qpj]] – BaPT + CTRA<br /> | ||
| Line 80: | Line 83: | ||
*'''Phosphoenolpyruvate-protein phosphotransferase''' | *'''Phosphoenolpyruvate-protein phosphotransferase''' | ||
| + | **[[2hwg]] - EcPEP<br /> | ||
| + | **[[5t12]] - EcPEP N terminal (mutant)<br /> | ||
**[[3nbm]] – PEP lactose-specific IIBC – ''Streptococcus pneumoniae''<BR /> | **[[3nbm]] – PEP lactose-specific IIBC – ''Streptococcus pneumoniae''<BR /> | ||
**[[2l2q]] - PEP cellbiose-specific IIB – ''Borrelia burgdorferi'' – NMR<br /> | **[[2l2q]] - PEP cellbiose-specific IIB – ''Borrelia burgdorferi'' – NMR<br /> | ||
| Line 95: | Line 100: | ||
**[[1wcr]] - EcPEP diacetylchitobiose-specific IIA (mutant) – NMR<br /> | **[[1wcr]] - EcPEP diacetylchitobiose-specific IIA (mutant) – NMR<br /> | ||
**[[1h9c]] - EcPEP diacetylchitobiose-specific IIB – NMR<br /> | **[[1h9c]] - EcPEP diacetylchitobiose-specific IIB – NMR<br /> | ||
| - | **[[2hwg]] - EcPEP<br /> | ||
**[[3ipr]] – EfPEP gluconate-specific IIA<br /> | **[[3ipr]] – EfPEP gluconate-specific IIA<br /> | ||
**[[3bed]] - EfPEP mannose-specific IIA<br /> | **[[3bed]] - EfPEP mannose-specific IIA<br /> | ||
| - | **[[5t12]] - EcPEP N terminal (mutant)<br /> | ||
**[[1nrz]] - KpPEP sorbose-specific IIB<br /> | **[[1nrz]] - KpPEP sorbose-specific IIB<br /> | ||
**[[2hro]] – PEP – ''Staphylococcus carnosus''<br /> | **[[2hro]] – PEP – ''Staphylococcus carnosus''<br /> | ||
| Line 130: | Line 133: | ||
**[[5igh]] – EcMPT I <br /> | **[[5igh]] – EcMPT I <br /> | ||
**[[5igi]], [[5igj]], [[5igs]], [[5igt]] – EcMPT I + antibiotic + guanosine<br /> | **[[5igi]], [[5igj]], [[5igs]], [[5igt]] – EcMPT I + antibiotic + guanosine<br /> | ||
| - | **[[5igp]], [[5igr]] – EcMPT I + antibiotic + GDP | + | **[[5igp]], [[5igr]] – EcMPT I + antibiotic + GDP<br /> |
| - | + | ||
**[[5uxb]] – BfMPT II – ''Brachybacterium faecium'' <br /> | **[[5uxb]] – BfMPT II – ''Brachybacterium faecium'' <br /> | ||
**[[5uxd]] – BfMPT II + antibiotic<br /> | **[[5uxd]] – BfMPT II + antibiotic<br /> | ||
| + | **[[5uxa]], [[5igu]] – EcMPT II <br /> | ||
**[[5iwu]] – EcMPT II + antibiotic<br /> | **[[5iwu]] – EcMPT II + antibiotic<br /> | ||
**[[5ih1]], [[5igv]], [[5igw]], [[5igy]], [[5igz]] – EcMPT II + antibiotic + GDP<br /> | **[[5ih1]], [[5igv]], [[5igw]], [[5igy]], [[5igz]] – EcMPT II + antibiotic + GDP<br /> | ||
Revision as of 09:25, 21 November 2019
| |||||||||||
3D structures of phosphotransferase
Updated on 21-November-2019
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
- ↑ Noguchi N, Takada K, Katayama J, Emura A, Sasatsu M. Regulation of transcription of the mph(A) gene for macrolide 2'-phosphotransferase I in Escherichia coli: characterization of the regulatory gene mphR(A). J Bacteriol. 2000 Sep;182(18):5052-8. PMID:10960087
- ↑ Shiba T, Itoh H, Kameda A, Kobayashi K, Kawazoe Y, Noguchi T. Polyphosphate:AMP phosphotransferase as a polyphosphate-dependent nucleoside monophosphate kinase in Acinetobacter johnsonii 210A. J Bacteriol. 2005 Mar;187(5):1859-65. PMID:15716459 doi:http://dx.doi.org/10.1128/JB.187.5.1859-1865.2005
- ↑ 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
