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Difference between revisions of "Glycosyltransferase Family 138"
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'''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite> that contains a '''Fido''' domain <cite>Kinch2009</cite> (Fig. 1A). AvrB is different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Therefore, AvrB is a unique Fido protein that functions as a glycosyltransferase. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' (or dTDP-rhamnose ''in vitro'') '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response). | '''GT138''' family of glycosyltransferase is exemplified by '''AvrB''' <cite>Peng2024</cite> that contains a '''Fido''' domain <cite>Kinch2009</cite> (Fig. 1A). AvrB is different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation <cite>Yarbrough2009</cite>, phosphorylation <cite>Castro-Roa2013</cite>, UMPylation <cite>Feng2012</cite>, and phosphocholination <cite>Mukherjee2011, Campanacci2013</cite>. Therefore, AvrB is a unique Fido protein that functions as a glycosyltransferase. As a bacterial effector from the plant pathogen ''Pseudomonas syringae'', '''AvrB utilizes host UDP-rhamnose''' (or dTDP-rhamnose ''in vitro'') '''as a co-substrate to modify the host protein RIN4''' and causes the programmed cell death (namely hypersensitive response). | ||
| − | [[File:GT138-Fig1-V3. | + | [[File:GT138-Fig1-V3.jpg|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left) is found in diverse enzymes including AvrB (right), which is a distinct glycosyltransferase. ('''B''') Other known glycosyltransferases contain folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108. PDB codes are provided for representative structures.]] |
Revision as of 19:21, 5 February 2025
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| Glycosyltransferase Family GT138 | |
| Clan | Fido fold |
| Mechanism | Inverting |
| Active site residues | Known |
| CAZy DB link | |
| https://www.cazy.org/GT138.html | |
Substrate specificities
GT138 family of glycosyltransferase is exemplified by AvrB [1] that contains a Fido domain [2] (Fig. 1A). AvrB is different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation [3], phosphorylation [4], UMPylation [5], and phosphocholination [6, 7]. Therefore, AvrB is a unique Fido protein that functions as a glycosyltransferase. As a bacterial effector from the plant pathogen Pseudomonas syringae, AvrB utilizes host UDP-rhamnose (or dTDP-rhamnose in vitro) as a co-substrate to modify the host protein RIN4 and causes the programmed cell death (namely hypersensitive response).
Kinetics and Mechanism
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Catalytic Residues
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Three-dimensional structures
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Family Firsts
- First stereochemistry determination
- Content is to be added here.
- First catalytic nucleophile identification
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- First general acid/base residue identification
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- First 3-D structure
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References
- Peng W, Garcia N, Servage KA, Kohler JJ, Ready JM, Tomchick DR, Fernandez J, and Orth K. (2024). Pseudomonas effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4. Sci Adv. 2024;10(7):eadd5108. DOI:10.1126/sciadv.add5108 |
- Kinch LN, Yarbrough ML, Orth K, and Grishin NV. (2009). Fido, a novel AMPylation domain common to fic, doc, and AvrB. PLoS One. 2009;4(6):e5818. DOI:10.1371/journal.pone.0005818 |
- Yarbrough ML, Li Y, Kinch LN, Grishin NV, Ball HL, and Orth K. (2009). AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science. 2009;323(5911):269-72. DOI:10.1126/science.1166382 |
- Castro-Roa D, Garcia-Pino A, De Gieter S, van Nuland NAJ, Loris R, and Zenkin N. (2013). The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu. Nat Chem Biol. 2013;9(12):811-7. DOI:10.1038/nchembio.1364 |
- Feng F, Yang F, Rong W, Wu X, Zhang J, Chen S, He C, and Zhou JM. (2012). A Xanthomonas uridine 5'-monophosphate transferase inhibits plant immune kinases. Nature. 2012;485(7396):114-8. DOI:10.1038/nature10962 |
- Mukherjee S, Liu X, Arasaki K, McDonough J, Galán JE, and Roy CR. (2011). Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature. 2011;477(7362):103-6. DOI:10.1038/nature10335 |
- Campanacci V, Mukherjee S, Roy CR, and Cherfils J. (2013). Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain. EMBO J. 2013;32(10):1469-77. DOI:10.1038/emboj.2013.82 |