1foa
From Proteopedia
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===CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I=== | ===CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I=== | ||
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{{ABSTRACT_PUBMED_11032794}} | {{ABSTRACT_PUBMED_11032794}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1foa]] is a 1 chain structure of [[O-GlcNAc transferase]] with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOA OCA]. | |
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| + | ==See Also== | ||
| + | *[[O-GlcNAc transferase|O-GlcNAc transferase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:011032794</ref><ref group="xtra">PMID:011467936</ref><ref group="xtra">PMID:019229296</ref><references group="xtra"/> |
[[Category: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase]] | [[Category: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
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[[Category: Donor substrate and metal ion complex]] | [[Category: Donor substrate and metal ion complex]] | ||
[[Category: N-acetylglucosaminyltransferase i]] | [[Category: N-acetylglucosaminyltransferase i]] | ||
| - | + | [[Category: Transferase]] | |
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Revision as of 07:13, 26 July 2012
Contents |
CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I
Template:ABSTRACT PUBMED 11032794
About this Structure
1foa is a 1 chain structure of O-GlcNAc transferase with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
See Also
Reference
- Unligil UM, Zhou S, Yuwaraj S, Sarkar M, Schachter H, Rini JM. X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily. EMBO J. 2000 Oct 16;19(20):5269-80. PMID:11032794 doi:10.1093/emboj/19.20.5269
- Chen W, Unligil UM, Rini JM, Stanley P. Independent Lec1A CHO glycosylation mutants arise from point mutations in N-acetylglucosaminyltransferase I that reduce affinity for both substrates. Molecular consequences based on the crystal structure of GlcNAc-TI. Biochemistry. 2001 Jul 31;40(30):8765-72. PMID:11467936
- Aksyuk AA, Leiman PG, Kurochkina LP, Shneider MM, Kostyuchenko VA, Mesyanzhinov VV, Rossmann MG. The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria. EMBO J. 2009 Apr 8;28(7):821-9. Epub 2009 Feb 19. PMID:19229296 doi:http://dx.doi.org/10.1038/emboj.2009.36
Categories: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase | Oryctolagus cuniculus | Rini, J M. | Sarkar, M. | Schachter, H. | Unligil, U M. | Yuwaraj, S. | Zhou, S. | 2-n-acetylglucosaminyltransferase | 3-mannosyl-glycoprotein | Alpha-1 | Beta-1 | Donor substrate and metal ion complex | N-acetylglucosaminyltransferase i | Transferase
