|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
18
|
|
pubmed:dateCreated |
2002-9-4
|
|
pubmed:databankReference |
|
|
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.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-10937989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-10937990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-10937997,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11013226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11058136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11283358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11296253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11373685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11470897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11483524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11517305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11680840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11680845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11828326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-11988470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-14222897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-14270536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-2023922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-2470511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-2682263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-5288752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-5329275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-5341411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-5760565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-7020753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-7529560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-7566085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-9242921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-9476894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-9535658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-9657144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12185246-9769102
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
3
|
|
pubmed:volume |
99
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
11670-5
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
|
|
pubmed:year |
2002
|
|
pubmed:articleTitle |
Structural insights into peptide bond formation.
|
|
pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520-8114, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
