2og5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2og5.gif|left|200px]] | [[Image:2og5.gif|left|200px]] | ||
'''Crystal structure of asparagine oxygenase (AsnO)''' | {{Structure | ||
|PDB= 2og5 |SIZE=350|CAPTION= <scene name='initialview01'>2og5</scene>, resolution 1.450Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | |||
|ACTIVITY= | |||
|GENE= sco3236 (asnO) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 Streptomyces coelicolor]) | |||
}} | |||
'''Crystal structure of asparagine oxygenase (AsnO)''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2OG5 is a [ | 2OG5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OG5 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17373765 17373765] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces coelicolor]] | [[Category: Streptomyces coelicolor]] | ||
| Line 17: | Line 26: | ||
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: NA]] | [[Category: NA]] | ||
[[Category: beta-hydroxylation of amino | [[Category: beta-hydroxylation of amino acid]] | ||
[[Category: iron(ii)/alpha-ketoglutarate dependent hydroxylase]] | [[Category: iron(ii)/alpha-ketoglutarate dependent hydroxylase]] | ||
[[Category: jelly-roll fold]] | [[Category: jelly-roll fold]] | ||
[[Category: non-ribosomal peptide synthesis]] | [[Category: non-ribosomal peptide synthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:59:16 2008'' | ||
Revision as of 15:59, 20 March 2008
| |||||||||||||
| 2og5, resolution 1.450Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | NA and ACY | ||||||||||||
| Gene: | sco3236 (asnO) (Streptomyces coelicolor) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of asparagine oxygenase (AsnO)
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
2OG5 is a Single protein structure of sequence from Streptomyces coelicolor. 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
Page seeded by OCA on Thu Mar 20 17:59:16 2008
