2chn
From Proteopedia
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| - | [[Image:2chn.gif|left|200px]]<br /> | + | [[Image:2chn.gif|left|200px]]<br /><applet load="2chn" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2chn" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2chn, resolution 1.95Å" /> | caption="2chn, resolution 1.95Å" /> | ||
'''BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY- NAG-THIAZOLINE COMPLEX'''<br /> | '''BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY- NAG-THIAZOLINE COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CHN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron Bacteroides thetaiotaomicron] with CA, NGT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] | + | 2CHN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron Bacteroides thetaiotaomicron] with CA, NGT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CHN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: o-glcnacase]] | [[Category: o-glcnacase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:23:10 2007'' |
Revision as of 17:13, 18 December 2007
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BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY- NAG-THIAZOLINE COMPLEX
Overview
O-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.
About this Structure
2CHN is a Protein complex structure of sequences from Bacteroides thetaiotaomicron with CA, NGT and GOL as ligands. Active as Beta-N-acetylhexosaminidase, with EC number 3.2.1.52 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
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