1kqs
From Proteopedia
(New page: 200px<br /><applet load="1kqs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kqs, resolution 3.10Å" /> '''The Haloarcula maris...) |
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| - | [[Image:1kqs.gif|left|200px]]<br /><applet load="1kqs" size=" | + | [[Image:1kqs.gif|left|200px]]<br /><applet load="1kqs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kqs, resolution 3.10Å" /> | caption="1kqs, resolution 3.10Å" /> | ||
'''The Haloarcula marismortui 50S Complexed with a Pretranslocational Intermediate in Protein Synthesis'''<br /> | '''The Haloarcula marismortui 50S Complexed with a Pretranslocational Intermediate in Protein Synthesis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The large ribosomal subunit catalyzes peptide bond formation during | + | The large ribosomal subunit catalyzes peptide bond formation during protein synthesis. Its peptidyl transferase activity has often been studied using a 'fragment assay' that depends on high concentrations of methanol or ethanol. Here we describe a version of this assay that does not require alcohol and use it to show, both crystallographically and biochemically, that crystals of the large ribosomal subunits from Haloarcula marismortui are enzymatically active. Addition of these crystals to solutions containing substrates results in formation of products, which ceases when crystals are removed. When substrates are diffused into large subunit crystals, the subsequent structure shows that products have formed. The CC-puromycin-peptide product is found bound to the A-site and the deacylated CCA is bound to the P-site, with its 3prime prime or minute OH near N3 A2486 (Escherichia coli A2451). Thus, this structure represents a state that occurs after peptide bond formation but before the hybrid state of protein synthesis. |
==About this Structure== | ==About this Structure== | ||
| - | 1KQS 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 MG, K, NA, CD, CL, PPU, PHA, ACA and BTN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1KQS 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=MG:'>MG</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=PPU:'>PPU</scene>, <scene name='pdbligand=PHA:'>PHA</scene>, <scene name='pdbligand=ACA:'>ACA</scene> and <scene name='pdbligand=BTN:'>BTN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Freeborn, B.]] | [[Category: Freeborn, B.]] | ||
| - | [[Category: Hansen, J | + | [[Category: Hansen, J L.]] |
| - | [[Category: Moore, P | + | [[Category: Moore, P B.]] |
| - | [[Category: Scaringe, S | + | [[Category: Scaringe, S A.]] |
| - | [[Category: Schmeing, T | + | [[Category: Schmeing, T M.]] |
| - | [[Category: Seila, A | + | [[Category: Seila, A C.]] |
| - | [[Category: Soukup, J | + | [[Category: Soukup, J K.]] |
| - | [[Category: Steitz, T | + | [[Category: Steitz, T A.]] |
| - | [[Category: Strobel, S | + | [[Category: Strobel, S A.]] |
[[Category: ACA]] | [[Category: ACA]] | ||
[[Category: BTN]] | [[Category: BTN]] | ||
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[[Category: rna-rna]] | [[Category: rna-rna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:57 2008'' |
Revision as of 11:37, 21 February 2008
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The Haloarcula marismortui 50S Complexed with a Pretranslocational Intermediate in Protein Synthesis
Overview
The large ribosomal subunit catalyzes peptide bond formation during protein synthesis. Its peptidyl transferase activity has often been studied using a 'fragment assay' that depends on high concentrations of methanol or ethanol. Here we describe a version of this assay that does not require alcohol and use it to show, both crystallographically and biochemically, that crystals of the large ribosomal subunits from Haloarcula marismortui are enzymatically active. Addition of these crystals to solutions containing substrates results in formation of products, which ceases when crystals are removed. When substrates are diffused into large subunit crystals, the subsequent structure shows that products have formed. The CC-puromycin-peptide product is found bound to the A-site and the deacylated CCA is bound to the P-site, with its 3prime prime or minute OH near N3 A2486 (Escherichia coli A2451). Thus, this structure represents a state that occurs after peptide bond formation but before the hybrid state of protein synthesis.
About this Structure
1KQS is a Protein complex structure of sequences from Haloarcula marismortui with , , , , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits., Schmeing TM, Seila AC, Hansen JL, Freeborn B, Soukup JK, Scaringe SA, Strobel SA, Moore PB, Steitz TA, Nat Struct Biol. 2002 Mar;9(3):225-30. PMID:11828326
Page seeded by OCA on Thu Feb 21 13:36:57 2008
Categories: Haloarcula marismortui | Protein complex | Freeborn, B. | Hansen, J L. | Moore, P B. | Scaringe, S A. | Schmeing, T M. | Seila, A C. | Soukup, J K. | Steitz, T A. | Strobel, S A. | ACA | BTN | CD | CL | K | MG | NA | PHA | PPU | Peptidyl transferase | Protein synthesis | Protein-protein | Protein-rna | Ribosome assembly | Rna-rna
