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4e1k

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'''Unreleased structure'''
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{{STRUCTURE_4e1k| PDB=4e1k | SCENE= }}
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===GlmU in complex with a Quinazoline Compound===
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{{ABSTRACT_PUBMED_22721802}}
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The entry 4e1k is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/GLMU_HAEIN GLMU_HAEIN]] 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:18029420</ref>
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Authors: Larsen, N.A., Doig, P.
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==About this Structure==
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[[4e1k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae_rd_kw20 Haemophilus influenzae rd kw20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1K OCA].
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Description: GlmU in complex with a Quinazoline Compound
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==Reference==
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<ref group="xtra">PMID:022721802</ref><references group="xtra"/><references/>
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[[Category: Haemophilus influenzae rd kw20]]
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[[Category: Doig, P.]]
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[[Category: Larsen, N A.]]
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[[Category: Acyltransferase]]
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[[Category: Cell shape]]
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[[Category: Cell wall biogenesis/degradation]]
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[[Category: Metal-binding]]
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[[Category: Multifunctional enzyme]]
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[[Category: Nucleotidyl transferase]]
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[[Category: Peptidoglycan synthesis]]
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[[Category: Transferase-transferase inhibitor complex]]
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[[Category: Uridyltransferase]]

Revision as of 16:03, 19 June 2013

Template:STRUCTURE 4e1k

Contents

GlmU in complex with a Quinazoline Compound

Template:ABSTRACT PUBMED 22721802

Function

[GLMU_HAEIN] 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]

About this Structure

4e1k is a 1 chain structure with sequence from Haemophilus influenzae rd kw20. Full crystallographic information is available from OCA.

Reference

  • Larsen NA, Nash TJ, Morningstar M, Shapiro AB, Joubran C, Blackett CJ, Patten AD, Boriack-Sjodin PA, Doig P. An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode. Biochem J. 2012 Sep 15;446(3):405-13. doi: 10.1042/BJ20120596. PMID:22721802 doi:10.1042/BJ20120596
  1. ↑ Mochalkin I, Lightle S, Zhu Y, Ohren JF, Spessard C, Chirgadze NY, Banotai C, Melnick M, McDowell L. Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU). Protein Sci. 2007 Dec;16(12):2657-66. PMID:18029420 doi:http://dx.doi.org/16/12/2657

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