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2gah
From Proteopedia
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|PDB= 2gah |SIZE=350|CAPTION= <scene name='initialview01'>2gah</scene>, resolution 2.00Å | |PDB= 2gah |SIZE=350|CAPTION= <scene name='initialview01'>2gah</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=FOA:2-FUROIC+ACID'>FOA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |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]) | |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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2gag|2GAG]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gah OCA], [http://www.ebi.ac.uk/pdbsum/2gah PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gah RCSB]</span> | ||
}} | }} | ||
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[[Category: Mathews, F S.]] | [[Category: Mathews, F S.]] | ||
[[Category: Zhao, G.]] | [[Category: Zhao, G.]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: FMN]] | ||
| - | [[Category: FOA]] | ||
| - | [[Category: NAD]] | ||
| - | [[Category: ZN]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
[[Category: flavoenzyme]] | [[Category: flavoenzyme]] | ||
| Line 37: | Line 35: | ||
[[Category: sarcosine oxidase]] | [[Category: sarcosine oxidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:14:07 2008'' |
Revision as of 00:14, 31 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Gene: | soxA (Stenotrophomonas maltophilia), soxB (Stenotrophomonas maltophilia), soxG (Stenotrophomonas maltophilia), soxD (Stenotrophomonas maltophilia) | ||||||
| Related: | 2GAG
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Heterotetrameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution
Overview
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 Structure
2GAH is a Protein complex structure of sequences from Stenotrophomonas maltophilia. Full crystallographic information is available from OCA.
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:16820168
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