2j65
From Proteopedia
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| - | [[Image:2j65. | + | [[Image:2j65.jpg|left|200px]]<br /><applet load="2j65" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2j65" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2j65, resolution 2.20Å" /> | caption="2j65, resolution 2.20Å" /> | ||
'''STRUCTURE OF LPXC FROM AQUIFEX AEOLICUS IN COMPLEX WITH UDP'''<br /> | '''STRUCTURE OF LPXC FROM AQUIFEX AEOLICUS IN COMPLEX WITH UDP'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2J65 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with ZN, CL, MYR and UDP as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 2J65 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with ZN, CL, MYR and UDP as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Myr Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J65 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: lipid synthesis]] | [[Category: lipid synthesis]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:50:36 2007'' |
Revision as of 17:40, 18 December 2007
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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 ZN, CL, MYR and UDP 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 Crystallograph 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 Tue Dec 18 19:50:36 2007
Categories: Aquifex aeolicus | Single protein | Buetow, L. | Dawson, A. | Hunter, W.N. | CL | MYR | UDP | ZN | Hydrolase | Lipid a biosynthesis | Lipid synthesis
