2j65: Difference between revisions
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|PDB= 2j65 |SIZE=350|CAPTION= <scene name='initialview01'>2j65</scene>, resolution 2.20Å | |PDB= 2j65 |SIZE=350|CAPTION= <scene name='initialview01'>2j65</scene>, resolution 2.20Å | ||
|SITE= <scene name='pdbsite=AC1:Myr+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Myr+Binding+Site+For+Chain+B'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene> and <scene name='pdbligand=UDP:URIDINE-5 | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene> and <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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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 Sun Mar 23 15:24:30 2008'' | ||
Revision as of 16:24, 23 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF LPXC FROM AQUIFEX AEOLICUS IN COMPLEX WITH UDP
OverviewOverview
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 StructureAbout this Structure
2J65 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
ReferenceReference
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
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