1y7l
From Proteopedia
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|PDB= 1y7l |SIZE=350|CAPTION= <scene name='initialview01'>1y7l</scene>, resolution 1.55Å | |PDB= 1y7l |SIZE=350|CAPTION= <scene name='initialview01'>1y7l</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] </span> |
|GENE= cysk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | |GENE= cysk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y7l OCA], [http://www.ebi.ac.uk/pdbsum/1y7l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y7l RCSB]</span> | ||
}} | }} | ||
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[[Category: Roderick, S L.]] | [[Category: Roderick, S L.]] | ||
[[Category: Vetting, M W.]] | [[Category: Vetting, M W.]] | ||
| - | [[Category: | + | [[Category: sulfhydrylase]] |
| - | [[Category: x-ray crystallography | + | [[Category: x-ray crystallography]] |
| - | ''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 00:59:47 2008'' |
Revision as of 21:59, 30 March 2008
| |||||||
| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | cysk (Haemophilus influenzae) | ||||||
| Activity: | Cysteine synthase, with EC number 2.5.1.47 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
O-Acetylserine Sulfhydrylase Complex
Overview
The biosynthesis of cysteine in bacteria and plants is carried out by a two-step pathway, catalyzed by serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS; O-acetylserine [thiol] lyase). The aerobic form of OASS forms a tight bienzyme complex with SAT in vivo, termed cysteine synthase. We have determined the crystal structure of OASS in complex with a C-terminal peptide of SAT required for bienzyme complex formation. The binding site of the peptide is at the active site of OASS, and its C-terminal carboxyl group occupies the same anion binding pocket as the alpha-carboxylate of the O-acetylserine substrate of OASS. These results explain the partial inhibition of OASS by SAT on complex formation as well as the competitive dissociation of the complex by O-acetylserine.
About this Structure
1Y7L is a Protein complex structure of sequences from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase., Huang B, Vetting MW, Roderick SL, J Bacteriol. 2005 May;187(9):3201-5. PMID:15838047
Page seeded by OCA on Mon Mar 31 00:59:47 2008
