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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2005-4-19
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-10052138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-10331874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-10452898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-10617639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-10993149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-11023792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-11055390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-11168407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-11388466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-11567162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-12081500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-12627979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-13990617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-14696376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-15073190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-15147185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-15231846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-15313214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-15333931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-15581365,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-15581568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-359557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-4891157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-4977445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-5332668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15838047-9761678
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
187
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3201-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2005
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pubmed:articleTitle |
The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase.
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pubmed:affiliation |
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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