1zch
From Proteopedia
(New page: 200px<br /><applet load="1zch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zch, resolution 1.85Å" /> '''Structure of the hyp...) |
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| - | [[Image:1zch.jpg|left|200px]]<br /><applet load="1zch" size=" | + | [[Image:1zch.jpg|left|200px]]<br /><applet load="1zch" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zch, resolution 1.85Å" /> | caption="1zch, resolution 1.85Å" /> | ||
'''Structure of the hypothetical oxidoreductase YcnD from Bacillus subtilis'''<br /> | '''Structure of the hypothetical oxidoreductase YcnD from Bacillus subtilis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | YcnD from the gram-positive bacterium Bacillus subtilis is a member of a | + | YcnD from the gram-positive bacterium Bacillus subtilis is a member of a family of bacterial proteins that act as NADH- and/or NADPH-dependent oxidoreductases. Here, we report for the first time on the biochemical characterization of the purified protein, demonstrating that YcnD is an FMN-containing enzyme that can be reduced by NADH or NADPH (Km = 6.4 and 4.4 microM, respectively). In the presence of free FMN as the electron-accepting substrate, the latter reductant showed a ping-pong Bi-Bi reaction mechanism, whereas utilization of NADH is competitively inhibited by this substrate. This finding suggests that NADPH is the physiological reductant of the enzyme. We also show that YcnD reduces nitro-organic compounds, chromate, and a series of azo dyes. The reduction of azo dyes appears to be mediated by free reduced FMN because the reaction is considerably slower in its absence. Structure determination by X-ray crystallography revealed that YcnD folds into a three layer alpha-beta-alpha sandwich strongly resembling the topology of the NADH oxidase superfamily. Similar to homologous bacterial oxidoreductase, YcnD forms homodimers with an extended dimer interface. The biochemical data and the structure are discussed in light of the putative physiological function of YcnD as an oxidoreductase delivering reduced FMN to enzymes that require the reduced cofactor for activity. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with CL, CA and FMN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1ZCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fitzpatrick, T | + | [[Category: Fitzpatrick, T B.]] |
[[Category: Gruber, K.]] | [[Category: Gruber, K.]] | ||
[[Category: Kratky, C.]] | [[Category: Kratky, C.]] | ||
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[[Category: nitroreductase]] | [[Category: nitroreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:11 2008'' |
Revision as of 14:14, 21 February 2008
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Structure of the hypothetical oxidoreductase YcnD from Bacillus subtilis
Overview
YcnD from the gram-positive bacterium Bacillus subtilis is a member of a family of bacterial proteins that act as NADH- and/or NADPH-dependent oxidoreductases. Here, we report for the first time on the biochemical characterization of the purified protein, demonstrating that YcnD is an FMN-containing enzyme that can be reduced by NADH or NADPH (Km = 6.4 and 4.4 microM, respectively). In the presence of free FMN as the electron-accepting substrate, the latter reductant showed a ping-pong Bi-Bi reaction mechanism, whereas utilization of NADH is competitively inhibited by this substrate. This finding suggests that NADPH is the physiological reductant of the enzyme. We also show that YcnD reduces nitro-organic compounds, chromate, and a series of azo dyes. The reduction of azo dyes appears to be mediated by free reduced FMN because the reaction is considerably slower in its absence. Structure determination by X-ray crystallography revealed that YcnD folds into a three layer alpha-beta-alpha sandwich strongly resembling the topology of the NADH oxidase superfamily. Similar to homologous bacterial oxidoreductase, YcnD forms homodimers with an extended dimer interface. The biochemical data and the structure are discussed in light of the putative physiological function of YcnD as an oxidoreductase delivering reduced FMN to enzymes that require the reduced cofactor for activity.
About this Structure
1ZCH is a Single protein structure of sequence from Bacillus subtilis with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure and function of YcnD from Bacillus subtilis, a flavin-containing oxidoreductase., Morokutti A, Lyskowski A, Sollner S, Pointner E, Fitzpatrick TB, Kratky C, Gruber K, Macheroux P, Biochemistry. 2005 Oct 25;44(42):13724-33. PMID:16229462
Page seeded by OCA on Thu Feb 21 16:14:11 2008
Categories: Bacillus subtilis | Single protein | Fitzpatrick, T B. | Gruber, K. | Kratky, C. | Lyskowski, A. | Macheroux, P. | Morokutti, A. | Pointner, E. | Sollner, S. | CA | CL | FMN | Nadh-oxidase | Nitroreductase
