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1y7l

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[[Image:1y7l.gif|left|200px]]
[[Image:1y7l.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1y7l |SIZE=350|CAPTION= <scene name='initialview01'>1y7l</scene>, resolution 1.55&Aring;
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The line below this paragraph, containing "STRUCTURE_1y7l", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|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>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= cysk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae])
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-->
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|DOMAIN=
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{{STRUCTURE_1y7l| PDB=1y7l | SCENE= }}
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|RELATEDENTRY=
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|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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}}
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'''O-Acetylserine Sulfhydrylase Complex'''
'''O-Acetylserine Sulfhydrylase Complex'''
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[[Category: Roderick, S L.]]
[[Category: Roderick, S L.]]
[[Category: Vetting, M W.]]
[[Category: Vetting, M W.]]
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[[Category: sulfhydrylase]]
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[[Category: Sulfhydrylase]]
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[[Category: x-ray crystallography]]
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[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:58:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:59:47 2008''
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Revision as of 12:58, 3 May 2008

Image:1y7l.gif

Template:STRUCTURE 1y7l

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 Sat May 3 15:58:02 2008

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