From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2bvg.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2bvg.jpg|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2bvg| PDB=2bvg | SCENE= }} | | {{STRUCTURE_2bvg| PDB=2bvg | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF 6-HYDOXY-D-NICOTINE OXIDASE FROM ARTHROBACTER NICOTINOVORANS. CRYSTAL FORM 1 (P21)'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16095622}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16095622 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_16095622}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| | [[Category: Nicotine degradation]] | | [[Category: Nicotine degradation]] |
| | [[Category: Oxidase]] | | [[Category: Oxidase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:51:29 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:20:53 2008'' |
Revision as of 15:20, 28 July 2008
Template:STRUCTURE 2bvg
CRYSTAL STRUCTURE OF 6-HYDOXY-D-NICOTINE OXIDASE FROM ARTHROBACTER NICOTINOVORANS. CRYSTAL FORM 1 (P21)
Template:ABSTRACT PUBMED 16095622
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 Mon Jul 28 18:20:53 2008
