1y7l
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1y7l.gif|left|200px]] | + | [[Image:1y7l.gif|left|200px]] |
| - | + | ||
| - | '''O-Acetylserine Sulfhydrylase Complex''' | + | {{Structure |
| + | |PDB= 1y7l |SIZE=350|CAPTION= <scene name='initialview01'>1y7l</scene>, resolution 1.55Å | ||
| + | |SITE= | ||
| + | |LIGAND= <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] | ||
| + | |GENE= cysk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | ||
| + | }} | ||
| + | |||
| + | '''O-Acetylserine Sulfhydrylase Complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1Y7L is a [ | + | 1Y7L is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y7L OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15838047 15838047] |
[[Category: Cysteine synthase]] | [[Category: Cysteine synthase]] | ||
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
| Line 20: | Line 29: | ||
[[Category: x-ray crystallography; sulfhydrylase]] | [[Category: x-ray crystallography; sulfhydrylase]] | ||
| - | ''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 15:19:23 2008'' |
Revision as of 13:19, 20 March 2008
| |||||||
| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | cysk (Haemophilus influenzae) | ||||||
| Activity: | Cysteine synthase, with EC number 2.5.1.47 | ||||||
| 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 Thu Mar 20 15:19:23 2008
