1y7l

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[[Image:1y7l.gif|left|200px]]
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{{STRUCTURE_1y7l| PDB=1y7l | SCENE= }}
{{STRUCTURE_1y7l| PDB=1y7l | SCENE= }}
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'''O-Acetylserine Sulfhydrylase Complex'''
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===O-Acetylserine Sulfhydrylase Complex===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15838047 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15838047}}
==About this Structure==
==About this Structure==
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[[Category: Sulfhydrylase]]
[[Category: Sulfhydrylase]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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Revision as of 11:21, 27 July 2008

Template:STRUCTURE 1y7l

O-Acetylserine Sulfhydrylase Complex

Template:ABSTRACT PUBMED 15838047

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

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