2cho: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity== | ==Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity== | ||
<StructureSection load='2cho' size='340' side='right' caption='[[2cho]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='2cho' size='340' side='right'caption='[[2cho]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cho]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bactn Bactn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHO FirstGlance]. <br> | <table><tr><td colspan='2'>[[2cho]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bactn Bactn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHO FirstGlance]. <br> | ||
| Line 37: | Line 37: | ||
[[Category: Bactn]] | [[Category: Bactn]] | ||
[[Category: Beta-N-acetylhexosaminidase]] | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Large Structures]] | |||
[[Category: Black, G N]] | [[Category: Black, G N]] | ||
[[Category: Davies, G J]] | [[Category: Davies, G J]] | ||
Revision as of 13:54, 26 February 2020
Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activityBacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity
Structural highlights
Function[OGA_BACTN] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedO-GlcNAc is an abundant post-translational modification of serine and threonine residues of nucleocytoplasmic proteins. This modification, found only within higher eukaryotes, is a dynamic modification that is often reciprocal to phosphorylation. In a manner analogous to phosphatases, a glycoside hydrolase termed O-GlcNAcase cleaves O-GlcNAc from modified proteins. Enzymes with high sequence similarity to human O-GlcNAcase are also found in human pathogens and symbionts. We report the three-dimensional structure of O-GlcNAcase from the human gut symbiont Bacteroides thetaiotaomicron both in its native form and in complex with a mimic of the reaction intermediate. Mutagenesis and kinetics studies show that the bacterial enzyme, very similarly to its human counterpart, operates via an unusual 'substrate-assisted' catalytic mechanism, which will inform the rational design of enzyme inhibitors. Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity.,Dennis RJ, Taylor EJ, Macauley MS, Stubbs KA, Turkenburg JP, Hart SJ, Black GN, Vocadlo DJ, Davies GJ Nat Struct Mol Biol. 2006 Apr;13(4):365-71. Epub 2006 Mar 26. PMID:16565725[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||||