1y56
From Proteopedia
(New page: 200px<br /><applet load="1y56" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y56, resolution 2.86Å" /> '''Crystal structure of...) |
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| - | [[Image:1y56.gif|left|200px]]<br /><applet load="1y56" size=" | + | [[Image:1y56.gif|left|200px]]<br /><applet load="1y56" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y56, resolution 2.86Å" /> | caption="1y56, resolution 2.86Å" /> | ||
'''Crystal structure of L-proline dehydrogenase from P.horikoshii'''<br /> | '''Crystal structure of L-proline dehydrogenase from P.horikoshii'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two novel types of dye-linked L-proline dehydrogenase complex (PDH1 and | + | Two novel types of dye-linked L-proline dehydrogenase complex (PDH1 and PDH2) were found in a hyperthermophilic archaeon, Pyrococcus horikoshii OT3. Here we report the first crystal structure of PDH1, which is a heterooctameric complex (alphabeta)4 containing three different cofactors: FAD, FMN, and ATP. The structure was determined by x-ray crystallography to a resolution of 2.86 angstroms. The structure of the beta subunit, which is an L-proline dehydrogenase catalytic component containing FAD as a cofactor, was similar to that of monomeric sarcosine oxidase. On the other hand, the alpha subunit possessed a unique structure composed of a classical dinucleotide fold domain with ATP, a central domain, an N-terminal domain, and a Cys-clustered domain. Serving as a third cofactor, FMN was located at the interface between the alpha and beta subunits in a novel configuration. The observed structure suggests that FAD and FMN are incorporated into an electron transfer system, with electrons passing from the former to the latter. The function of ATP is unknown, but it may play a regulatory role. Although the structure of the alpha subunit differs from that of the beta subunit, except for the presence of an analogous dinucleotide domain with a different cofactor, the structural characteristics of PDH1 suggest that each represents a divergent enzyme that arose from a common ancestral flavoenzyme and that they eventually formed a complex to gain a new function. The structural characteristics described here reveal the PDH1 complex to be a unique diflavin dehydrogenase containing a novel electron transfer system. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y56 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii_ot3 Pyrococcus horikoshii ot3] with FE, CL, SO4, FAD, FMN, ATP and CXS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Proline_dehydrogenase Proline dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.8 1.5.99.8] Full crystallographic information is available from [http:// | + | 1Y56 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii_ot3 Pyrococcus horikoshii ot3] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=FMN:'>FMN</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=CXS:'>CXS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Proline_dehydrogenase Proline dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.8 1.5.99.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y56 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:52 2008'' |
Revision as of 14:01, 21 February 2008
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Crystal structure of L-proline dehydrogenase from P.horikoshii
Overview
Two novel types of dye-linked L-proline dehydrogenase complex (PDH1 and PDH2) were found in a hyperthermophilic archaeon, Pyrococcus horikoshii OT3. Here we report the first crystal structure of PDH1, which is a heterooctameric complex (alphabeta)4 containing three different cofactors: FAD, FMN, and ATP. The structure was determined by x-ray crystallography to a resolution of 2.86 angstroms. The structure of the beta subunit, which is an L-proline dehydrogenase catalytic component containing FAD as a cofactor, was similar to that of monomeric sarcosine oxidase. On the other hand, the alpha subunit possessed a unique structure composed of a classical dinucleotide fold domain with ATP, a central domain, an N-terminal domain, and a Cys-clustered domain. Serving as a third cofactor, FMN was located at the interface between the alpha and beta subunits in a novel configuration. The observed structure suggests that FAD and FMN are incorporated into an electron transfer system, with electrons passing from the former to the latter. The function of ATP is unknown, but it may play a regulatory role. Although the structure of the alpha subunit differs from that of the beta subunit, except for the presence of an analogous dinucleotide domain with a different cofactor, the structural characteristics of PDH1 suggest that each represents a divergent enzyme that arose from a common ancestral flavoenzyme and that they eventually formed a complex to gain a new function. The structural characteristics described here reveal the PDH1 complex to be a unique diflavin dehydrogenase containing a novel electron transfer system.
About this Structure
1Y56 is a Protein complex structure of sequences from Pyrococcus horikoshii ot3 with , , , , , and as ligands. Active as Proline dehydrogenase, with EC number 1.5.99.8 Full crystallographic information is available from OCA.
Reference
Crystal structure of a novel FAD-, FMN-, and ATP-containing L-proline dehydrogenase complex from Pyrococcus horikoshii., Tsuge H, Kawakami R, Sakuraba H, Ago H, Miyano M, Aki K, Katunuma N, Ohshima T, J Biol Chem. 2005 Sep 2;280(35):31045-9. Epub 2005 Jul 15. PMID:16027125
Page seeded by OCA on Thu Feb 21 16:01:52 2008
Categories: Proline dehydrogenase | Protein complex | Pyrococcus horikoshii ot3 | Ago, H. | Aki, K. | Katunuma, N. | Kawakami, R. | Miyano, M. | Ohshima, T. | Sakuraba, H. | Tsuge, H. | ATP | CL | CXS | FAD | FE | FMN | SO4 | Dehydrogenase | Protein-protein complex
