2bvg
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2bvg.gif|left|200px]] | + | [[Image:2bvg.gif|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF 6-HYDOXY-D-NICOTINE OXIDASE FROM ARTHROBACTER NICOTINOVORANS. CRYSTAL FORM 1 (P21)''' | + | {{Structure |
| + | |PDB= 2bvg |SIZE=350|CAPTION= <scene name='initialview01'>2bvg</scene>, resolution 3.18Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+D'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/(R)-6-hydroxynicotine_oxidase (R)-6-hydroxynicotine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.6 1.5.3.6] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF 6-HYDOXY-D-NICOTINE OXIDASE FROM ARTHROBACTER NICOTINOVORANS. CRYSTAL FORM 1 (P21)''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2BVG is a [ | + | 2BVG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_nicotinovorans Arthrobacter nicotinovorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVG OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans., Koetter JW, Schulz GE, J Mol Biol. 2005 Sep 16;352(2):418-28. PMID:[http:// | + | Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans., Koetter JW, Schulz GE, J Mol Biol. 2005 Sep 16;352(2):418-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16095622 16095622] |
[[Category: (R)-6-hydroxynicotine oxidase]] | [[Category: (R)-6-hydroxynicotine oxidase]] | ||
[[Category: Arthrobacter nicotinovorans]] | [[Category: Arthrobacter nicotinovorans]] | ||
| Line 18: | Line 27: | ||
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: autoflavinylation]] | [[Category: autoflavinylation]] | ||
| - | [[Category: enantiomeric | + | [[Category: enantiomeric substrate]] |
| - | [[Category: | + | [[Category: flavoenzyme]] |
[[Category: nicotine degradation]] | [[Category: nicotine degradation]] | ||
[[Category: oxidase]] | [[Category: oxidase]] | ||
| - | ''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 16:07:15 2008'' |
Revision as of 14:07, 20 March 2008
| |||||||
| , resolution 3.18Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | (R)-6-hydroxynicotine oxidase, with EC number 1.5.3.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF 6-HYDOXY-D-NICOTINE OXIDASE FROM ARTHROBACTER NICOTINOVORANS. CRYSTAL FORM 1 (P21)
Overview
The crystal structure of 6-hydroxy-d-nicotine oxidase (EC 1.5.3.6) was solved by X-ray diffraction analysis in three crystal forms at resolutions up to 1.9 A. The enzyme is monomeric in solution and also in the mother liquor but formed disulfide-dimers in all crystals. It belongs to the p-cresol methylhydroxylase-vanillyl-alcohol oxidase family and contains an FAD covalently bound to the polypeptide. The covalent bond of this enzyme was the first for which a purely autocatalytic formation had been shown. In contrast to previous reports, the bond does not involve N(epsilon2) (N3) of His72 but the N(delta1) (N1) atom. The geometry of this reaction is proposed and the autoflavinylation is discussed in the light of homologous structures. The enzyme is specific for 6-hydroxy-D-nicotine and is inhibited by the L-enantiomer. This observation was verified by modeling enzyme-substrate and enzyme-inhibitor complexes, which also showed the geometry of the catalyzed reaction. The binding models indicated that the deprotonation of the substrate rather than the hydride transfer is the specificity-determining step. The functionally closely related 6-hydroxy-L-nicotine oxidase processing the L-enantiomer is sequence-related to the greater glutathione reductase family with quite a different chainfold. A model of this "sister enzyme" derived from known homologous structures suggests that the reported L-substrate specificity and D-enantiomer inhibition are also determined by the location of the deprotonating base.
About this Structure
2BVG is a Single protein structure of sequence from Arthrobacter nicotinovorans. Full crystallographic information is available from OCA.
Reference
Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans., Koetter JW, Schulz GE, J Mol Biol. 2005 Sep 16;352(2):418-28. PMID:16095622
Page seeded by OCA on Thu Mar 20 16:07:15 2008
