2j65
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structure of recombinant Aquifex aeolicus | + | The structure of recombinant Aquifex aeolicus UDP-3-O-acyl-N-acetylglucosamine deacetylase (LpxC) in complex with UDP has been determined to a resolution of 2.2 A. Previous studies have characterized the binding sites of the fatty-acid and sugar moieties of the substrate, UDP-(3-O-hydroxymyristoyl)-N-acetylglucosamine, but not that of the nucleotide. The uracil-binding site is constructed from amino acids that are highly conserved across species. Hydrophobic associations with the Phe155 and Arg250 side chains in combination with hydrogen-bonding interactions with the main chain of Glu154 and the side chains of Tyr151 and Lys227 position the base. The phosphate and ribose groups are directed away from the active site and interact with Arg137, Lys156, Glu186 and Arg250. The orientation of the phosphate-ribose tail is not conducive to catalysis, perhaps owing to the position of an inhibitory Zn(2+). However, based on the position of uracil revealed in this study and on the previously reported complex of LpxC with an inhibitor, a model is proposed for substrate binding. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | The nucleotide-binding site of Aquifex aeolicus LpxC., Buetow L, Dawson A, Hunter WN, Acta | + | The nucleotide-binding site of Aquifex aeolicus LpxC., Buetow L, Dawson A, Hunter WN, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1082-6. Epub 2006 Oct 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17077484 17077484] |
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Buetow, L.]] | [[Category: Buetow, L.]] | ||
[[Category: Dawson, A.]] | [[Category: Dawson, A.]] | ||
| - | [[Category: Hunter, W | + | [[Category: Hunter, W N.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: MYR]] | [[Category: MYR]] | ||
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[[Category: lipid synthesis]] | [[Category: lipid synthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:59:41 2008'' |
Revision as of 15:59, 21 February 2008
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STRUCTURE OF LPXC FROM AQUIFEX AEOLICUS IN COMPLEX WITH UDP
Overview
The structure of recombinant Aquifex aeolicus UDP-3-O-acyl-N-acetylglucosamine deacetylase (LpxC) in complex with UDP has been determined to a resolution of 2.2 A. Previous studies have characterized the binding sites of the fatty-acid and sugar moieties of the substrate, UDP-(3-O-hydroxymyristoyl)-N-acetylglucosamine, but not that of the nucleotide. The uracil-binding site is constructed from amino acids that are highly conserved across species. Hydrophobic associations with the Phe155 and Arg250 side chains in combination with hydrogen-bonding interactions with the main chain of Glu154 and the side chains of Tyr151 and Lys227 position the base. The phosphate and ribose groups are directed away from the active site and interact with Arg137, Lys156, Glu186 and Arg250. The orientation of the phosphate-ribose tail is not conducive to catalysis, perhaps owing to the position of an inhibitory Zn(2+). However, based on the position of uracil revealed in this study and on the previously reported complex of LpxC with an inhibitor, a model is proposed for substrate binding.
About this Structure
2J65 is a Single protein structure of sequence from Aquifex aeolicus with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The nucleotide-binding site of Aquifex aeolicus LpxC., Buetow L, Dawson A, Hunter WN, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1082-6. Epub 2006 Oct 25. PMID:17077484
Page seeded by OCA on Thu Feb 21 17:59:41 2008
Categories: Aquifex aeolicus | Single protein | Buetow, L. | Dawson, A. | Hunter, W N. | CL | MYR | UDP | ZN | Hydrolase | Lipid a biosynthesis | Lipid synthesis
