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1q7y

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(New page: 200px<br /><applet load="1q7y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q7y, resolution 3.20&Aring;" /> '''Crystal Structure of...)
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[[Image:1q7y.gif|left|200px]]<br /><applet load="1q7y" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1q7y, resolution 3.20&Aring;" />
caption="1q7y, resolution 3.20&Aring;" />
'''Crystal Structure of CCdAP-Puromycin bound at the Peptidyl transferase center of the 50S ribosomal subunit'''<br />
'''Crystal Structure of CCdAP-Puromycin bound at the Peptidyl transferase center of the 50S ribosomal subunit'''<br />
==Overview==
==Overview==
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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.
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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==
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1Q7Y 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, PO4 and PUY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q7Y OCA].
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1Q7Y 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=PO4:'>PO4</scene> and <scene name='pdbligand=PUY:'>PUY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7Y OCA].
==Reference==
==Reference==
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[[Category: Haloarcula marismortui]]
[[Category: Haloarcula marismortui]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Hansen, J.L.]]
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[[Category: Hansen, J L.]]
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[[Category: Moore, P.B.]]
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[[Category: Moore, P B.]]
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[[Category: Schmeing, T.M.]]
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[[Category: Schmeing, T M.]]
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[[Category: Steitz, T.A.]]
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[[Category: Steitz, T A.]]
[[Category: CD]]
[[Category: CD]]
[[Category: CL]]
[[Category: CL]]
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[[Category: rna-rna complex]]
[[Category: rna-rna complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:27:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:46 2008''

Revision as of 12:36, 21 February 2008


1q7y, resolution 3.20Å

Drag the structure with the mouse to rotate

Crystal Structure of CCdAP-Puromycin bound at the Peptidyl transferase center of 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

1Q7Y 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 14:36:46 2008

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