1m90
From Proteopedia
(New page: 200px<br /><applet load="1m90" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m90, resolution 2.80Å" /> '''Co-crystal structure...) |
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| - | [[Image:1m90.gif|left|200px]]<br /><applet load="1m90" size=" | + | [[Image:1m90.gif|left|200px]]<br /><applet load="1m90" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m90, resolution 2.80Å" /> | caption="1m90, resolution 2.80Å" /> | ||
'''Co-crystal structure of CCA-Phe-caproic acid-biotin and sparsomycin bound to the 50S ribosomal subunit'''<br /> | '''Co-crystal structure of CCA-Phe-caproic acid-biotin and sparsomycin bound to the 50S ribosomal subunit'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The large ribosomal subunit catalyzes peptide bond formation and will do | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1M90 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui] with SPS, MG, NA, K, CD, CL, PHA and ACA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1M90 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui] with <scene name='pdbligand=SPS:'>SPS</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=PHA:'>PHA</scene> and <scene name='pdbligand=ACA:'>ACA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M90 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Haloarcula marismortui]] | [[Category: Haloarcula marismortui]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Hansen, J | + | [[Category: Hansen, J L.]] |
| - | [[Category: Moore, P | + | [[Category: Moore, P B.]] |
| - | [[Category: Schmeing, T | + | [[Category: Schmeing, T M.]] |
| - | [[Category: Steitz, T | + | [[Category: Steitz, T A.]] |
[[Category: ACA]] | [[Category: ACA]] | ||
[[Category: CD]] | [[Category: CD]] | ||
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[[Category: sparsomycin]] | [[Category: sparsomycin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:49 2008'' |
Revision as of 11:52, 21 February 2008
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Co-crystal structure of CCA-Phe-caproic acid-biotin and sparsomycin bound to the 50S ribosomal subunit
Overview
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.
About this Structure
1M90 is a Protein complex structure of sequences from Haloarcula marismortui with , , , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Structural insights into peptide bond formation., Hansen JL, Schmeing TM, Moore PB, Steitz TA, Proc Natl Acad Sci U S A. 2002 Sep 3;99(18):11670-5. Epub 2002 Aug 16. PMID:12185246
Page seeded by OCA on Thu Feb 21 13:52:49 2008
Categories: Haloarcula marismortui | Protein complex | Hansen, J L. | Moore, P B. | Schmeing, T M. | Steitz, T A. | ACA | CD | CL | K | MG | NA | PHA | SPS | P-site | Ribosome | Sparsomycin
