2oi5

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[[Image:2oi5.jpg|left|200px]]<br /><applet load="2oi5" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2oi5.jpg|left|200px]]
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caption="2oi5, resolution 2.25&Aring;" />
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'''E. coli GlmU- Complex with UDP-GlcNAc and Acetyl-CoA'''<br />
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{{Structure
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|PDB= 2oi5 |SIZE=350|CAPTION= <scene name='initialview01'>2oi5</scene>, resolution 2.25&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene> and <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene>
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|ACTIVITY=
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|GENE= glmU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''E. coli GlmU- Complex with UDP-GlcNAc and Acetyl-CoA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2OI5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ACO:'>ACO</scene> and <scene name='pdbligand=UD1:'>UD1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OI5 OCA].
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2OI5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OI5 OCA].
==Reference==
==Reference==
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Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products., Olsen LR, Vetting MW, Roderick SL, Protein Sci. 2007 Jun;16(6):1230-5. Epub 2007 May 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17473010 17473010]
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Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products., Olsen LR, Vetting MW, Roderick SL, Protein Sci. 2007 Jun;16(6):1230-5. Epub 2007 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17473010 17473010]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: left-handed beta helix]]
[[Category: left-handed beta helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:18:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:00:05 2008''

Revision as of 16:00, 20 March 2008


PDB ID 2oi5

Drag the structure with the mouse to rotate
, resolution 2.25Å
Ligands: , , and
Gene: glmU (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



E. coli GlmU- Complex with UDP-GlcNAc and Acetyl-CoA


Overview

The biosynthesis of UDP-GlcNAc in bacteria is carried out by GlmU, an essential bifunctional uridyltransferase that catalyzes the CoA-dependent acetylation of GlcN-1-PO(4) to form GlcNAc-1-PO(4) and its subsequent condensation with UTP to form pyrophosphate and UDP-GlcNAc. As a metabolite, UDP-GlcNAc is situated at a branch point leading to the biosynthesis of lipopolysaccharide and peptidoglycan. Consequently, GlmU is regarded as an important target for potential antibacterial agents. The crystal structure of the Escherichia coli GlmU acetyltransferase active site has been determined in complexes with acetyl-CoA, CoA/GlcN-1-PO(4), and desulpho-CoA/GlcNAc-1-PO(4). These structures reveal the enzyme groups responsible for binding the substrates. A superposition of these complex structures suggests that the 2-amino group of GlcN-1-PO(4) is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism.

About this Structure

2OI5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products., Olsen LR, Vetting MW, Roderick SL, Protein Sci. 2007 Jun;16(6):1230-5. Epub 2007 May 1. PMID:17473010

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