| pubmed-article:12185246 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12185246 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:12185246 | lifeskim:mentions | umls-concept:C0678616 | lld:lifeskim |
| pubmed-article:12185246 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12185246 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:12185246 | pubmed:dateCreated | 2002-9-4 | lld:pubmed |
| pubmed-article:12185246 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12185246 | pubmed:abstractText | The large ribosomal subunit catalyzes peptide bond formation and will do so by using small aminoacyl- and peptidyl-RNA fragments of tRNA. We have refined at 3-A resolution the structures of both A and P site substrate and product analogues, as well as an intermediate analogue, bound to the Haloarcula marismortui 50S ribosomal subunit. A P site substrate, CCA-Phe-caproic acid-biotin, binds equally to both sites, but in the presence of sparsomycin binds only to the P site. The CCA portions of these analogues are bound identically by either the A or P loop of the 23S rRNA. Combining the separate P and A site substrate complexes into one model reveals interactions that may occur when both are present simultaneously. The alpha-NH(2) group of an aminoacylated fragment in the A site forms one hydrogen bond with the N3 of A2486 (2451) and may form a second hydrogen bond either with the 2' OH of the A-76 ribose in the P site or with the 2' OH of A2486 (2451). These interactions position the alpha amino group adjacent to the carbonyl carbon of esterified P site substrate in an orientation suitable for a nucleophilic attack. | lld:pubmed |
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| pubmed-article:12185246 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12185246 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12185246 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12185246 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:12185246 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:12185246 | pubmed:author | pubmed-author:SchmeingT... | lld:pubmed |
| pubmed-article:12185246 | pubmed:author | pubmed-author:HansenJeffrey... | lld:pubmed |
| pubmed-article:12185246 | pubmed:author | pubmed-author:MoorePeter... | lld:pubmed |
| pubmed-article:12185246 | pubmed:author | pubmed-author:SteitzThomas... | lld:pubmed |
| pubmed-article:12185246 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12185246 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:12185246 | pubmed:volume | 99 | lld:pubmed |
| pubmed-article:12185246 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12185246 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12185246 | pubmed:pagination | 11670-5 | lld:pubmed |
| pubmed-article:12185246 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12185246 | pubmed:meshHeading | pubmed-meshheading:12185246... | lld:pubmed |
| pubmed-article:12185246 | pubmed:meshHeading | pubmed-meshheading:12185246... | lld:pubmed |
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| pubmed-article:12185246 | pubmed:meshHeading | pubmed-meshheading:12185246... | lld:pubmed |
| pubmed-article:12185246 | pubmed:meshHeading | pubmed-meshheading:12185246... | lld:pubmed |
| pubmed-article:12185246 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12185246 | pubmed:articleTitle | Structural insights into peptide bond formation. | lld:pubmed |
| pubmed-article:12185246 | pubmed:affiliation | Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520-8114, USA. | lld:pubmed |
| pubmed-article:12185246 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12185246 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12185246 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:12185246 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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