1y7l
From Proteopedia
(New page: 200px<br /><applet load="1y7l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y7l, resolution 1.55Å" /> '''O-Acetylserine Sulfh...) |
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| - | [[Image:1y7l.gif|left|200px]]<br /><applet load="1y7l" size=" | + | [[Image:1y7l.gif|left|200px]]<br /><applet load="1y7l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y7l, resolution 1.55Å" /> | caption="1y7l, resolution 1.55Å" /> | ||
'''O-Acetylserine Sulfhydrylase Complex'''<br /> | '''O-Acetylserine Sulfhydrylase Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The biosynthesis of cysteine in bacteria and plants is carried out by a | + | 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== | ==About this Structure== | ||
| - | 1Y7L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1Y7L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y7L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Huang, B.]] | [[Category: Huang, B.]] | ||
| - | [[Category: Roderick, S | + | [[Category: Roderick, S L.]] |
| - | [[Category: Vetting, M | + | [[Category: Vetting, M W.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: x-ray crystallography; sulfhydrylase]] | [[Category: x-ray crystallography; sulfhydrylase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:02:31 2008'' |
Revision as of 14:02, 21 February 2008
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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 with as ligand. Active as Cysteine synthase, with EC number 2.5.1.47 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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