2gag: Difference between revisions
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'''Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution''' | {{Structure | ||
|PDB= 2gag |SIZE=350|CAPTION= <scene name='initialview01'>2gag</scene>, resolution 1.85Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FOA:2-FUROIC+ACID'>FOA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= soxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40324 Stenotrophomonas maltophilia]), soxB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40324 Stenotrophomonas maltophilia]), soxG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40324 Stenotrophomonas maltophilia]), soxD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40324 Stenotrophomonas maltophilia]) | |||
}} | |||
'''Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2GAG is a [ | 2GAG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GAG OCA]. | ||
==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:// | 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] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Stenotrophomonas maltophilia]] | [[Category: Stenotrophomonas maltophilia]] | ||
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[[Category: sarcosine oxidase]] | [[Category: sarcosine oxidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:02:21 2008'' | ||
Revision as of 18:02, 20 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , and | ||||||
| Gene: | soxA (Stenotrophomonas maltophilia), soxB (Stenotrophomonas maltophilia), soxG (Stenotrophomonas maltophilia), soxD (Stenotrophomonas maltophilia) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution
OverviewOverview
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.
About this StructureAbout this Structure
2GAG is a Protein complex structure of sequences from Stenotrophomonas maltophilia. Full crystallographic information is available from OCA.
ReferenceReference
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:16820168
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