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| '''Heterotetrameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution'''
| | ===Heterotetrameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution=== |
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| ==Overview==
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| The crystal structure of heterotetrameric sarcosine oxidase (TSOX) from Pseudomonas maltophilia has been determined at 1.85 A resolution. TSOX contains three coenzymes (FAD, FMN and NAD+), four different subunits (alpha, 103 kDa; beta, 44 kDa; gamma, 21 kDa; delta, 11 kDa) and catalyzes the oxidation of sarcosine (N-methylglycine) to yield hydrogen peroxide, glycine and formaldehyde. In the presence of tetrahydrofolate, the oxidation of sarcosine is coupled to the formation of 5,10-methylenetetrahydrofolate. The NAD+ and putative folate binding sites are located in the alpha-subunit. The FAD binding site is in the beta-subunit. FMN is bound at the interface of the alpha and beta-subunits. The FAD and FMN rings are separated by a short segment of the beta-subunit with the closest atoms located 7.4 A apart. Sulfite, an inhibitor of oxygen reduction, is bound at the FMN site. 2-Furoate, a competitive inhibitor with respect to sarcosine, is bound at the FAD site. The sarcosine dehydrogenase and 5,10-methylenetetrahydrofolate synthase sites are 35 A apart but connected by a large internal cavity (approximately 10,000 A3). An unexpected zinc ion, coordinated by three cysteine and one histidine side-chains, is bound to the delta-subunit. The N-terminal half of the alpha subunit of TSOX (alphaA) is closely similar to the FAD-binding domain of glutathione reductase but with NAD+ replacing FAD. The C-terminal half of the alpha subunit of TSOX (alphaB) is similar to the C-terminal half of dimethylglycine oxidase and the T-protein of the glycine cleavage system, proteins that bind tetrahydrofolate. The beta-subunit of TSOX is very similar to monomeric sarcosine oxidase. The gamma-subunit is similar to the C-terminal sub-domain of alpha-TSOX. The delta-subunit shows little similarity with any PDB entry. The alphaA domain/beta-subunit sub-structure of TSOX closely resembles the alphabeta dimer of L-proline dehydrogenase, a heteroctameric protein (alphabeta)4 that shows highest overall similarity to TSOX.
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| | (as it appears on PubMed at http://www.pubmed.gov), where 16820168 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16820168}} |
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| ==About this Structure== | | ==About this Structure== |
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| ==Reference== | | ==Reference== |
| Heterotetrameric sarcosine oxidase: structure of a diflavin metalloenzyme at 1.85 A resolution., Chen ZW, Hassan-Abdulah A, Zhao G, Jorns MS, Mathews FS, J Mol Biol. 2006 Jul 28;360(5):1000-18. Epub 2006 Jun 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16820168 16820168] | | Heterotetrameric sarcosine oxidase: structure of a diflavin metalloenzyme at 1.85 A resolution., Chen ZW, Hassan-Abdulah A, Zhao G, Jorns MS, Mathews FS, J Mol Biol. 2006 Jul 28;360(5):1000-18. Epub 2006 Jun 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16820168 16820168] |
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| | Cloning, expression and crystallization of heterotetrameric sarcosine oxidase from Pseudomonas maltophilia., Hassan-Abdallah A, Zhao G, Eschenbrenner M, Chen ZW, Mathews FS, Jorns MS, Protein Expr Purif. 2005 Sep;43(1):33-43. Epub 2005 Apr 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15922624 15922624] |
| [[Category: Protein complex]] | | [[Category: Protein complex]] |
| [[Category: Stenotrophomonas maltophilia]] | | [[Category: Stenotrophomonas maltophilia]] |
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| [[Category: Folate-methylating enzyme]] | | [[Category: Folate-methylating enzyme]] |
| [[Category: Sarcosine oxidase]] | | [[Category: Sarcosine oxidase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:53:10 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:06:45 2008'' |