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| | {{STRUCTURE_2cdu| PDB=2cdu | SCENE= }} | | {{STRUCTURE_2cdu| PDB=2cdu | SCENE= }} |
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| - | '''THE CRYSTAL STRUCTURE OF WATER-FORMING NAD(P)H OXIDASE FROM LACTOBACILLUS SANFRANCISCENSIS'''
| + | ===THE CRYSTAL STRUCTURE OF WATER-FORMING NAD(P)H OXIDASE FROM LACTOBACILLUS SANFRANCISCENSIS=== |
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| - | ==Overview==
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| - | The FAD-dependent NAD(P)H oxidase from Lactobacillus sanfrancisensis (L.san-Nox2) catalyzes the oxidation of 2 equivalents of either NADH or NADPH and reduces 1 equivalent of O(2) to yield 2 equivalents of water. During steady-state turnover only 0.5% of the reducing equivalents are detected in solution as hydrogen peroxide, suggesting that it is not released from the enzyme after the oxidation of the first equivalent of NAD(P)H and reaction with O(2). Here we report the crystal structure of L.san-Nox2 to 1.8 A resolution. The enzyme crystallizes as a dimer with each monomer consisting of a FAD binding domain (residues 1-120), a NAD(P)H binding domain (residues 150-250), and a dimerization domain (residues 325-451). The electron density for the redox-active Cys42 residue located adjacent to the si-face FAD is consistent with oxidation to the sulfenic acid (Cys-SOH) state. The side chain of Cys42 is also observed in two conformations; in one the sulfenic acid is hydrogen bonded to His10 and in the other it hydrogen bonds with the FAD O2' atom. Surprisingly, the NAD(P)H binding domains each contain an ADP ligand as established by electron density maps and MALDI-TOF analysis of the ligands released from heat-denatured enzyme. The ADP ligand copurifies with the enzyme, and its presence does not inhibit enzyme activity. Consequently, we hypothesize that either NADPH or NADH substrates bind via a long channel that extends from the enzyme exterior and terminates at the FAD re-face. A homology model of the NADH oxidase from Lactococcus lactis (L.lac-Nox2) was also generated using the crystal structure of L.san-Nox2, which reveals several important similarities and differences between the two enzymes. HPLC analysis of ligands released from denatured L.lac-Nox2 indicates that it does not bind ADP, which correlates with the specificity of the enzyme for oxidation of NADH.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16893166}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16893166 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16893166}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Flavoenzyme]] | | [[Category: Flavoenzyme]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:54:08 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:29:36 2008'' |
Revision as of 12:29, 29 July 2008
Template:STRUCTURE 2cdu
THE CRYSTAL STRUCTURE OF WATER-FORMING NAD(P)H OXIDASE FROM LACTOBACILLUS SANFRANCISCENSIS
Template:ABSTRACT PUBMED 16893166
About this Structure
2CDU is a Single protein structure of sequence from Lactobacillus sanfranciscensis. Full crystallographic information is available from OCA.
Reference
The crystal structure of NAD(P)H oxidase from Lactobacillus sanfranciscensis: insights into the conversion of O2 into two water molecules by the flavoenzyme., Lountos GT, Jiang R, Wellborn WB, Thaler TL, Bommarius AS, Orville AM, Biochemistry. 2006 Aug 15;45(32):9648-59. PMID:16893166
Page seeded by OCA on Tue Jul 29 15:29:36 2008
