2og6
From Proteopedia
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|PDB= 2og6 |SIZE=350|CAPTION= <scene name='initialview01'>2og6</scene>, resolution 1.916Å | |PDB= 2og6 |SIZE=350|CAPTION= <scene name='initialview01'>2og6</scene>, resolution 1.916Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= sco3236 (asnO) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2 Bacteria]) | |GENE= sco3236 (asnO) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2 Bacteria]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2og5|2OG5]], [[2og7|2OG7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2og6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2og6 OCA], [http://www.ebi.ac.uk/pdbsum/2og6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2og6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Essen, L O.]] | [[Category: Essen, L O.]] | ||
[[Category: Strieker, M.]] | [[Category: Strieker, M.]] | ||
| - | [[Category: | + | [[Category: alpha-ketoglutarate oxygenase]] |
| - | [[Category: | + | [[Category: beta-hydroxylated amino acid]] |
| - | [[Category: | + | [[Category: non-heme iron(ii)]] |
| + | [[Category: nonribosomal peptide synthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:17:20 2008'' |
Revision as of 01:17, 31 March 2008
| |||||||
| , resolution 1.916Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | sco3236 (asnO) (Bacteria) | ||||||
| Related: | 2OG5, 2OG7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of asparagine oxygenase in complex with Fe(II)
Overview
Non-ribosomally synthesized lipopeptide antibiotics of the daptomycin type are known to contain unnatural beta-modified amino acids, which are essential for bioactivity. Here we present the biochemical and structural basis for the incorporation of 3-hydroxyasparagine at position 9 in the 11-residue acidic lipopeptide lactone calcium-dependent antibiotic (CDA). Direct hydroxylation of l-asparagine by AsnO, a non-heme Fe(2+)/alpha-ketoglutarate-dependent oxygenase encoded by the CDA biosynthesis gene cluster, was validated by Fmoc derivatization of the reaction product and LC/MS analysis. The 1.45, 1.92, and 1.66 A crystal structures of AsnO as apoprotein, Fe(2+) complex, and product complex, respectively, with (2S,3S)-3-hydroxyasparagine and succinate revealed the stereoselectivity and substrate specificity of AsnO. The comparison of native and product-complex structures of AsnO showed a lid-like region (residues F208-E223) that seals the active site upon substrate binding and shields it from sterically demanding peptide substrates. Accordingly, beta-hydroxylated asparagine is synthesized prior to its incorporation into the growing CDA peptide. The AsnO structure could serve as a template for engineering novel enzymes for the synthesis of beta-hydroxylated amino acids.
About this Structure
2OG6 is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
Reference
Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide., Strieker M, Kopp F, Mahlert C, Essen LO, Marahiel MA, ACS Chem Biol. 2007 Mar 20;2(3):187-96. PMID:17373765
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