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1ybg

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[[Image:1ybg.gif|left|200px]]<br /><applet load="1ybg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ybg.gif|left|200px]]
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caption="1ybg, resolution 2.6&Aring;" />
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'''MurA inhibited by a derivative of 5-sulfonoxy-anthranilic acid'''<br />
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{{Structure
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|PDB= 1ybg |SIZE=350|CAPTION= <scene name='initialview01'>1ybg</scene>, resolution 2.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=TAV:N-METHYL-N-{2-[(2-NAPHTHYLSULFONYL)AMINO]-5-[(2-NAPHTHYLSULFONYL)OXY]BENZOYL}-L-ASPARTIC ACID'>TAV</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7]
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|GENE= murA, murZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=550 Enterobacter cloacae])
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}}
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'''MurA inhibited by a derivative of 5-sulfonoxy-anthranilic acid'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae] with <scene name='pdbligand=TAV:'>TAV</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBG OCA].
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1YBG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBG OCA].
==Reference==
==Reference==
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A novel inhibitor that suspends the induced fit mechanism of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA)., Eschenburg S, Priestman MA, Abdul-Latif FA, Delachaume C, Fassy F, Schonbrunn E, J Biol Chem. 2005 Apr 8;280(14):14070-5. Epub 2005 Feb 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15701635 15701635]
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A novel inhibitor that suspends the induced fit mechanism of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA)., Eschenburg S, Priestman MA, Abdul-Latif FA, Delachaume C, Fassy F, Schonbrunn E, J Biol Chem. 2005 Apr 8;280(14):14070-5. Epub 2005 Feb 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15701635 15701635]
[[Category: Enterobacter cloacae]]
[[Category: Enterobacter cloacae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: inside-out alpha-beta barrel]]
[[Category: inside-out alpha-beta barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:20:44 2008''

Revision as of 13:20, 20 March 2008


PDB ID 1ybg

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands:
Gene: murA, murZ (Enterobacter cloacae)
Activity: UDP-N-acetylglucosamine 1-carboxyvinyltransferase, with EC number 2.5.1.7
Coordinates: save as pdb, mmCIF, xml



MurA inhibited by a derivative of 5-sulfonoxy-anthranilic acid


Overview

MurA (UDP-N-acetylglucosamine enolpyruvyl transferase, EC 2.5.1.7) catalyzes the first committed step in the synthesis of the bacterial cell wall. It is the target of the naturally occurring, broad-spectrum antibiotic fosfomycin. Fosfomycin, an epoxide, is a relatively poor drug because an ever-increasing number of bacteria have developed resistance to fosfomycin. Thus, there is a critical need for the development of novel drugs that target MurA by a different molecular mode of action. We have identified a new scaffold of potent MurA inhibitors, derivatives of 5-sulfonoxy-anthranilic acid, using high-throughput screening. T6361 and T6362 are competitive inhibitors of MurA with respect to the first substrate, UDP-N-acetylglucosamine (UNAG), with a K(i) of 16 microM. The crystal structure of the MurA.T6361 complex at 2.6 angstrom resolution, together with fluorescence data, revealed that the inhibitor targets a loop, Pro112 to Pro121, that is crucial for the structural changes of the enzyme during catalysis. Thus, this new class of MurA inhibitors is not active site-directed but instead obstructs the transition from the open (unliganded) to the closed (UNAG-liganded) enzyme form. The results provide evidence for the existence of a MurA.UNAG collision complex that may be specifically targeted by small molecules different from ground-state analogs of the enzymatic reaction.

About this Structure

1YBG is a Single protein structure of sequence from Enterobacter cloacae. Full crystallographic information is available from OCA.

Reference

A novel inhibitor that suspends the induced fit mechanism of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA)., Eschenburg S, Priestman MA, Abdul-Latif FA, Delachaume C, Fassy F, Schonbrunn E, J Biol Chem. 2005 Apr 8;280(14):14070-5. Epub 2005 Feb 8. PMID:15701635

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