Phosphotransferase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 51: Line 51:
**[[3sgc]], [[3n4t]], [[3n4u]], [[3n4v]] ,[[4dbx]], [[4de4]] - EncAGPT ID – ''Enterococcus casseliflavus''<BR />
**[[3sgc]], [[3n4t]], [[3n4u]], [[3n4v]] ,[[4dbx]], [[4de4]] - EncAGPT ID – ''Enterococcus casseliflavus''<BR />
**[[1j7i]] - EfAGPT IIIA <br />
**[[1j7i]] - EfAGPT IIIA <br />
-
**[[4h05]] – PT VIII – ''Streptomyces rimosus''<br />
+
**[[4h05]], [[6fuc]] – PT VIII – ''Streptomyces rimosus''<br />
**[[4pdy]] – PT – ''Alicyclobacillus acidocaldarius''<br />
**[[4pdy]] – PT – ''Alicyclobacillus acidocaldarius''<br />
 +
**[[6ef6]] – PT – ''Mycobacterium smegmatis''<br />
*Aminoglycoside phosphotransferase complex with nucleotide
*Aminoglycoside phosphotransferase complex with nucleotide
Line 75: Line 76:
**[[3sg8]], [[3sg9]], [[4dfb]], [[4dfu]] - EncAGPT ID + antibiotic<br />
**[[3sg8]], [[3sg9]], [[4dfb]], [[4dfu]] - EncAGPT ID + antibiotic<br />
**[[3i0o]] - LpAGPT IA + ADP + antibiotic<br />
**[[3i0o]] - LpAGPT IA + ADP + antibiotic<br />
-
**[[4feu]], [[4fev]], [[4few]], [[4fex]], [[4gkh]], [[4gki]] - LpAGPT IA + inhibitor + antibiotic
+
**[[4feu]], [[4fev]], [[4few]], [[4fex]], [[4gkh]], [[4gki]] - LpAGPT IA + inhibitor + antibiotic<br />
 +
**[[6fux]] - SrAGPT + ADP + antibiotic<br />
*Aminoglycoside phosphotransferase complex with inhibitor
*Aminoglycoside phosphotransferase complex with inhibitor
Line 128: Line 130:
**[[2jvi]], [[2jvj]], [[2jvk]] - BsPT Spo0F (mutant) – NMR<br />
**[[2jvi]], [[2jvj]], [[2jvk]] - BsPT Spo0F (mutant) – NMR<br />
**[[3q15]] - BsPT spo0F + response regulator aspartate phosphatase<br />
**[[3q15]] - BsPT spo0F + response regulator aspartate phosphatase<br />
 +
**[[6ifh]] – SpoF - ''Paenisporosarcina''<br />
*'''Microlide 2”-phosphotransferase'''
*'''Microlide 2”-phosphotransferase'''
Line 141: Line 144:
**[[5ih0]] – EcMPT II (mutant) + antibiotic + GDP<br />
**[[5ih0]] – EcMPT II (mutant) + antibiotic + GDP<br />
-
*'''Polyphospate:AMP phosphotransferase or polyphosphate kinase'''
+
*'''Polyphosphate:AMP phosphotransferase or polyphosphate kinase'''
**[[5lc9]] – MrPAPT – ''Meiothermus ruber'' <br />
**[[5lc9]] – MrPAPT – ''Meiothermus ruber'' <br />
Line 149: Line 152:
**[[5o6m]] – MrPAPT (mutant) + ATP <br />
**[[5o6m]] – MrPAPT (mutant) + ATP <br />
**[[5ldb]], [[5maq]] – MrPAPT + ADP <br />
**[[5ldb]], [[5maq]] – MrPAPT + ADP <br />
 +
**[[6dzg]] – PAPT + ADP – ''Rhizobium meliloti''<br />
 +
**[[6au0]], [[6aqn]] – ChPAPT + inhibitor – ''Cytophaga hutchinsonii'' <br />
 +
**[[6anh]] – ChPAPT + guanosine tetraphosphate <br />
 +
**[[6ang]] – ChPAPT + AMP <br />
 +
**[[6an9]] – ChPAPT + ADP <br />
*Rifampin phosphotransferase
*Rifampin phosphotransferase

Revision as of 09:58, 21 November 2019

Aminoglycoside phosphotransferase complex with gentamycin, and glycerol (PDB entry 3ham)

Drag the structure with the mouse to rotate

3D structures of phosphotransferase

Updated on 21-November-2019

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. 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
  5. 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
  6. 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Personal tools