This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox UNLPam 12
From Proteopedia
(Difference between revisions)
(New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...) |
|||
| (3 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | == | + | ==Active Site and Laminarin Binding In Glycoside Hydrolase Family 55== |
| - | <StructureSection load=' | + | <StructureSection load='4PEW' size='380' side='right' caption='SacteLam55A is a GH55 enzyme from Streptomyces sp. SirexAA-E. (PDB entry [[4PEW]])' scene='71/719629/Sactelam55a/1'> |
| - | + | ||
| - | + | The Carbohydrate Active Enzyme(CaZY) database indicates that glycoside hydrolase family 55 (GH55) contains both endo- and exo-β -1,3-glucanases.We present high resolution crystal structures of bacterial SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E with bound substrates and product. These structures, along with mutagenesis and kinetic studies implicate Glu502 as the catalytic acid and a proton relay network of four residues in activating water as the nucleophile. Further, a set of conserved aromatic residues that define the active site apparently enforce an exo-glucanase reactivity as demonstrated by exhaustive hydrolysis reactions with purified laminarioligosaccharides. Two additional aromatic residues that line the substratebinding channel show substrate-dependent conformational flexibility that may promote processive reactivity of the bound oligosaccharide in the bacterial enzymes. | |
== Function == | == Function == | ||
SacteLam55A is a GH55 enzyme from highly cellulolytic Streptomyces sp. SirexAA-E. Substrate bound structures identify residues involved in binding, catalysis, enforcement of reaction specificity and possibly processivity. Natural GH55 are exo-β-1,3- glucanases with a broad range of temperature and | SacteLam55A is a GH55 enzyme from highly cellulolytic Streptomyces sp. SirexAA-E. Substrate bound structures identify residues involved in binding, catalysis, enforcement of reaction specificity and possibly processivity. Natural GH55 are exo-β-1,3- glucanases with a broad range of temperature and | ||
pH optima. | pH optima. | ||
| - | |||
== Relevance == | == Relevance == | ||
| Line 16: | Line 15: | ||
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
| - | </StructureSection> | ||
== References == | == References == | ||
| - | + | Christopher M. Bianchetti, Taichi E. Takasuka, Sam Deutsch, Hannah S. Udell, Eric J. Yik, Lai F. Bergeman, and Brian G. Fox. | |
| - | + | ||
| + | </StructureSection> | ||
Current revision
Active Site and Laminarin Binding In Glycoside Hydrolase Family 55
| |||||||||||
