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Difference between revisions of "Glycoside Hydrolase Family 164"
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== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | To date the structure of only one GH164 has been solved, from Bacteroidetes salyersiae β-mannosidase (Bs164). Bs164 exists as a donut shaped trimer, see figure 1A. Each trimer-donut has an outer diameter of approximately 100 Å and an internal diameter of between 30 and 35 Å. The individual Bs164 chains contain three clearly defined domains: a modified (β/α)8 barrel, a domain containing a seven membered mixed β-sheet sandwiched between α-helices, and a β-sheet domain (Figure 1B). This domain architecture is quite similar to that seen for family [[GH42]] enzymes <cite> | + | To date the structure of only one GH164 has been solved, from Bacteroidetes salyersiae β-mannosidase (Bs164). Bs164 exists as a donut shaped trimer, see figure 1A. Each trimer-donut has an outer diameter of approximately 100 Å and an internal diameter of between 30 and 35 Å. The individual Bs164 chains contain three clearly defined domains: a modified (β/α)8 barrel, a domain containing a seven membered mixed β-sheet sandwiched between α-helices, and a β-sheet domain (Figure 1B). This domain architecture is quite similar to that seen for family [[GH42]] enzymes <cite>Hidaka2002<cite>, but is previously unseen for β-mannosidases. |
[[Image:BS164_AB.png|thumb|right|450px|'''Figure 1. '''The trimeric structure of Bs164 is shown in panel''' A'''. All three protomers are shown with a surface and each chain is displayed as a cartoon diagram coloured by domain.''' B '''shows the structure of one protomer. Domain A, which has a (β/α)8 fold, is shown in green with subdomain H is shown in magenta, domain B, containing a mixed β-sheet, is shown in red and the β-sandwich of domain C is shown in blue.''' ''']] | [[Image:BS164_AB.png|thumb|right|450px|'''Figure 1. '''The trimeric structure of Bs164 is shown in panel''' A'''. All three protomers are shown with a surface and each chain is displayed as a cartoon diagram coloured by domain.''' B '''shows the structure of one protomer. Domain A, which has a (β/α)8 fold, is shown in green with subdomain H is shown in magenta, domain B, containing a mixed β-sheet, is shown in red and the β-sandwich of domain C is shown in blue.''' ''']] | ||
| Line 52: | Line 52: | ||
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #Hidaka2002 pmid=12215416 |
| − | |||
#Armstrong2020 pmid=31871050 | #Armstrong2020 pmid=31871050 | ||
Revision as of 10:09, 2 April 2020
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.
- Author: ^^^Zachary Armstrong^^^
- Responsible Curator: ^^^Gideon Davies^^^
| Glycoside Hydrolase Family GH164 | |
| Clan | GH-x |
| Mechanism | retaining/inverting |
| Active site residues | known/not known |
| CAZy DB link | |
| https://www.cazy.org/GH164.html | |
Substrate specificities
Content is to be added here.
Authors may get an idea of what to put in each field from Curator Approved Glycoside Hydrolase Families. (TIP: Right click with your mouse and open this link in a new browser window...)
In the meantime, please see these references for an essential introduction to the CAZy classification system: [1, 2].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
To date the structure of only one GH164 has been solved, from Bacteroidetes salyersiae β-mannosidase (Bs164). Bs164 exists as a donut shaped trimer, see figure 1A. Each trimer-donut has an outer diameter of approximately 100 Å and an internal diameter of between 30 and 35 Å. The individual Bs164 chains contain three clearly defined domains: a modified (β/α)8 barrel, a domain containing a seven membered mixed β-sheet sandwiched between α-helices, and a β-sheet domain (Figure 1B). This domain architecture is quite similar to that seen for family GH42 enzymes [3, 4, 4, 5, 6, 6, 6, 6, 6, 6, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 21, 22, 22, 22, 23, 24, 24, 24, 24, 24, 24, 25, 25, 25, 25, 25, 26, 27, 27, 28, 29, 30, 31, 32, 32, 33, 33, 33, 33, 34, 35, 35, 36, 37, 38, 39, 40, 41, 42, 43, 43, 44, 44, 44, 45, 45, 46, 47, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75]
- First catalytic nucleophile identification
- Bacteroides salyersiae β-mannosidase by 2-fluoromannose labeling and kinetic analysis of mutants [75]
- First general acid/base residue identification
- Bacteroides salyersiae β-mannosidase by kinetic analysis of mutants [75]
- First 3-D structure of a GH1 enzyme
- Bacteroides salyersiae β-mannosidase [75]
References
- Hidaka M, Fushinobu S, Ohtsu N, Motoshima H, Matsuzawa H, Shoun H, and Wakagi T. (2002). Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose. J Mol Biol. 2002;322(1):79-91. DOI:10.1016/s0022-2836(02)00746-5 |
- Armstrong Z and Davies GJ. (2020). Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164. J Biol Chem. 2020;295(13):4316-4326. DOI:10.1074/jbc.RA119.011591 |