4hcq
From Proteopedia
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{{STRUCTURE_4hcq| PDB=4hcq | SCENE= }} | {{STRUCTURE_4hcq| PDB=4hcq | SCENE= }} | ||
===Crystal structure of GLMU from mycobacterium tuberculosis in complex with glucosamine-1-phosphate=== | ===Crystal structure of GLMU from mycobacterium tuberculosis in complex with glucosamine-1-phosphate=== | ||
+ | {{ABSTRACT_PUBMED_23485416}} | ||
+ | |||
+ | ==Function== | ||
+ | [[http://www.uniprot.org/uniprot/GLMU_MYCTU GLMU_MYCTU]] Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.<ref>PMID:19237750</ref> <ref>PMID:19121323</ref> | ||
==About this Structure== | ==About this Structure== | ||
[[4hcq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HCQ OCA]. | [[4hcq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HCQ OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:023485416</ref><references group="xtra"/><references/> | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Jagtap, P K.A.]] | [[Category: Jagtap, P K.A.]] |
Revision as of 14:09, 10 July 2013
Contents |
Crystal structure of GLMU from mycobacterium tuberculosis in complex with glucosamine-1-phosphate
Template:ABSTRACT PUBMED 23485416
Function
[GLMU_MYCTU] Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.[1] [2]
About this Structure
4hcq is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
- Jagtap PK, Verma SK, Vithani N, Bais VS, Prakash B. Crystal structures identify an atypical two-metal-ion mechanism for uridyltransfer in GlmU: its significance to sugar nucleotidyl transferases. J Mol Biol. 2013 May 27;425(10):1745-59. doi: 10.1016/j.jmb.2013.02.019. Epub, 2013 Feb 26. PMID:23485416 doi:10.1016/j.jmb.2013.02.019
- ↑ Zhang Z, Bulloch EM, Bunker RD, Baker EN, Squire CJ. Structure and function of GlmU from Mycobacterium tuberculosis. Acta Crystallogr D Biol Crystallogr. 2009 Mar;65(Pt 3):275-83. Epub 2009, Feb 20. PMID:19237750 doi:10.1107/S0907444909001036
- ↑ Parikh A, Verma SK, Khan S, Prakash B, Nandicoori VK. PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity. J Mol Biol. 2009 Feb 20;386(2):451-64. Epub 2008 Dec 24. PMID:19121323 doi:10.1016/j.jmb.2008.12.031
Categories: Mycobacterium tuberculosis | Jagtap, P K.A. | Verma, S K. | Vithani, N. | Acetyltransferase | Acyltransferase | Bifunctional | Cell shape | Cell wall biogenesis/degradation | Left-handed-beta-helix | Magnesium | Metal-binding | Multifunctional enzyme | Nucleotidyltransferase | Peptidoglycan synthesis | Pyrophosphorylase | Rossmann-like fold | Transferase