pubmed-article:12878593 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12878593 | lifeskim:mentions | umls-concept:C0010546 | lld:lifeskim |
pubmed-article:12878593 | lifeskim:mentions | umls-concept:C0003995 | lld:lifeskim |
pubmed-article:12878593 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:12878593 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
pubmed-article:12878593 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
pubmed-article:12878593 | lifeskim:mentions | umls-concept:C0376437 | lld:lifeskim |
pubmed-article:12878593 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:12878593 | lifeskim:mentions | umls-concept:C1709061 | lld:lifeskim |
pubmed-article:12878593 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
pubmed-article:12878593 | pubmed:issue | 40 | lld:pubmed |
pubmed-article:12878593 | pubmed:dateCreated | 2003-9-29 | lld:pubmed |
pubmed-article:12878593 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12878593 | pubmed:abstractText | We have determined the crystal structure of a 154-residue intein derived from the dnaB gene of Synechocystis sp. strain PCC6803 and refined it to a 2.0-A resolution. The x-ray structure suggests that this intein possesses two catalytic sites that appear to be separately responsible for splicing and cleavage of the N- and C-terminal scissile bonds. The conserved intein block F residues are the important components of a catalytic site for side chain cyclization of the last intein residue, Asn-154. The data suggest that the imidazole ring of His-143 is involved in the activation of the side chain Ndelta atom of Asn-154, leading to a nucleophilic attack on the carbonyl carbon of Asn-154. Substitution of His-143 with Ala or Gln resulted in the inhibition of C-terminal cleavage. His-153, Asp-136, and a water molecule appear to constitute an oxyanion binding site by contacting the carbonyl oxygen of Asn-154 to stabilize the transition state. The structure and mutagenesis data also support that the close contact between the hydroxyl groups of Thr-138 and Ser-155, whose side chain participates in an S --> O acyl shift, plays an important role in the nucleophile orientation. Our structural modeling suggests that this catalytic module is conserved in the C-terminal subdomains of inteins from diverse organisms. | lld:pubmed |
pubmed-article:12878593 | pubmed:language | eng | lld:pubmed |
pubmed-article:12878593 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12878593 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12878593 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12878593 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12878593 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12878593 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12878593 | pubmed:month | Oct | lld:pubmed |
pubmed-article:12878593 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:12878593 | pubmed:author | pubmed-author:DingYiY | lld:pubmed |
pubmed-article:12878593 | pubmed:author | pubmed-author:RaoZiheZ | lld:pubmed |
pubmed-article:12878593 | pubmed:author | pubmed-author:ChenXuehuiX | lld:pubmed |
pubmed-article:12878593 | pubmed:author | pubmed-author:XuMing-QunMQ | lld:pubmed |
pubmed-article:12878593 | pubmed:author | pubmed-author:LesageGuillau... | lld:pubmed |
pubmed-article:12878593 | pubmed:author | pubmed-author:GhoshIncaI | lld:pubmed |
pubmed-article:12878593 | pubmed:author | pubmed-author:FerrandonSeba... | lld:pubmed |
pubmed-article:12878593 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12878593 | pubmed:day | 3 | lld:pubmed |
pubmed-article:12878593 | pubmed:volume | 278 | lld:pubmed |
pubmed-article:12878593 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12878593 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12878593 | pubmed:pagination | 39133-42 | lld:pubmed |
pubmed-article:12878593 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:12878593 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12878593 | pubmed:articleTitle | Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing. | lld:pubmed |
pubmed-article:12878593 | pubmed:affiliation | Laboratory of Structural Biology and the Ministry of Education Laboratory of Protein Science, School of Life Science and Engineering, Tsinghua University, Beijing 100084, People's Republic of China. | lld:pubmed |
pubmed-article:12878593 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12878593 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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