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Glucosamine 6-phosphate synthase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The sugar binding by G6PS induces conformational change of the enzyme domains. <scene name='51/516474/Cv/ | + | The sugar binding by G6PS induces conformational change of the enzyme domains. <scene name='51/516474/Cv/5'>Active site</scene>. The <scene name='51/516474/Cv/6'>sugar binding pocket</scene> is found in the interface between the synthase and the glutaminase domains of G6PS<ref>PMID:18295797</ref>. |
</StructureSection> | </StructureSection> | ||
==3D structures of glucosamine 6-phosphate synthase== | ==3D structures of glucosamine 6-phosphate synthase== | ||
Revision as of 13:06, 1 April 2019
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3D structures of glucosamine 6-phosphate synthase
Updated on 01-April-2019
2vf4 - EcG6PS – Escherichia coli
3tbf – G6PS C terminal – Francisella tularensis
1moq, 2vf5 – EcG6PS + G6P
1mor, 1jxa – EcG6PS + glucose 6-phosphate
1xff - EcG6PS glutaminase domain + glutamate
1xfg - EcG6PS glutaminase domain + glutamic hydroxamate
1mos – EcG6PS + ADGP
4amv – EcG6PS + F6P
2j6h - EcG6PS + oxo-norleucine + glucose 6-phosphate
References
- ↑ White SH, Wimley WC, Selsted ME. Structure, function, and membrane integration of defensins. Curr Opin Struct Biol. 1995 Aug;5(4):521-7. PMID:8528769
- ↑ Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B. Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel. J Mol Biol. 2008 Apr 4;377(4):1174-85. Epub 2008 Feb 4. PMID:18295797 doi:10.1016/j.jmb.2008.01.077
