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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>. 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>. 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). | ||
| − | AvrB contains a '''Fido''' domain <cite>Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Varki2022</cite> (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. | + | AvrB contains a '''Fido''' domain <cite>Kinch2009</cite> (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 <cite>Lairson2008, Varki2022</cite> (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. |
[[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) 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.]] | [[File:GT138-Fig1-V3.png|thumb|1300px|right|'''Figure 1. Glycosyltransferase folds.''' ('''A''') Fido fold (left <cite>Kinch2009</cite>) 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.]] | ||
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#Campanacci2013 pmid=23572077 | #Campanacci2013 pmid=23572077 | ||
#Varki2022 pmid=35536922 | #Varki2022 pmid=35536922 | ||
| − | # | + | #Lairson2008 pmid=18518825 |
</biblio> | </biblio> | ||
Revision as of 21:21, 10 February 2025
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
| 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]. 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).
AvrB contains a Fido domain [2] (Fig. 1A), different from other known glycosyltransferases containing folds of GT-A, GT-B, GT-C, lysozyme-type, GT101, and GT108 [3, 4] (Fig. 1B). Interestingly, Fido proteins can also be enzymes with activities of AMPylation [5], phosphorylation [6], UMPylation [7], and phosphocholination [8, 9]. Therefore, AvrB is a unique Fido protein that functions as a glycosyltransferase.
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
AvrB represents the prototype for glycosyltransferases of Fido fold. AvrB contains a relatively large internal domain between helix α2 and helix α3 (Fig. 1A). Other Fido enzyme structures have been determined, though they have diverse activities as mentioned above. These Fido proteins share a similar fold while the primary sequences are divergent.
Family Firsts
- First stereochemistry determination
- Content is to be added here.
- First catalytic nucleophile identification
- Content is to be added here.
- First general acid/base residue identification
- Content is to be added here.
- First 3-D structure
- Content is to be added here.
References
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- Lairson LL, Henrissat B, Davies GJ, and Withers SG. (2008). Glycosyltransferases: structures, functions, and mechanisms. Annu Rev Biochem. 2008;77:521-55. DOI:10.1146/annurev.biochem.76.061005.092322 |
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