1fg0: Difference between revisions
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[[Image:1fg0.gif|left|200px]] | [[Image:1fg0.gif|left|200px]] | ||
'''LARGE RIBOSOMAL SUBUNIT COMPLEXED WITH A 13 BP MINIHELIX-PUROMYCIN COMPOUND''' | {{Structure | ||
|PDB= 1fg0 |SIZE=350|CAPTION= <scene name='initialview01'>1fg0</scene>, resolution 3.00Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''LARGE RIBOSOMAL SUBUNIT COMPLEXED WITH A 13 BP MINIHELIX-PUROMYCIN COMPOUND''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FG0 is a [ | 1FG0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FG0 OCA]. | ||
==Reference== | ==Reference== | ||
The structural basis of ribosome activity in peptide bond synthesis., Nissen P, Hansen J, Ban N, Moore PB, Steitz TA, Science. 2000 Aug 11;289(5481):920-30. PMID:[http:// | The structural basis of ribosome activity in peptide bond synthesis., Nissen P, Hansen J, Ban N, Moore PB, Steitz TA, Science. 2000 Aug 11;289(5481):920-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10937990 10937990] | ||
[[Category: Haloarcula marismortui]] | [[Category: Haloarcula marismortui]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rna-rna]] | [[Category: rna-rna]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:08:35 2008'' | ||
Revision as of 12:08, 20 March 2008
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LARGE RIBOSOMAL SUBUNIT COMPLEXED WITH A 13 BP MINIHELIX-PUROMYCIN COMPOUND
OverviewOverview
Using the atomic structures of the large ribosomal subunit from Haloarcula marismortui and its complexes with two substrate analogs, we establish that the ribosome is a ribozyme and address the catalytic properties of its all-RNA active site. Both substrate analogs are contacted exclusively by conserved ribosomal RNA (rRNA) residues from domain V of 23S rRNA; there are no protein side-chain atoms closer than about 18 angstroms to the peptide bond being synthesized. The mechanism of peptide bond synthesis appears to resemble the reverse of the acylation step in serine proteases, with the base of A2486 (A2451 in Escherichia coli) playing the same general base role as histidine-57 in chymotrypsin. The unusual pK(a) (where K(a) is the acid dissociation constant) required for A2486 to perform this function may derive in part from its hydrogen bonding to G2482 (G2447 in E. coli), which also interacts with a buried phosphate that could stabilize unusual tautomers of these two bases. The polypeptide exit tunnel is largely formed by RNA but has significant contributions from proteins L4, L22, and L39e, and its exit is encircled by proteins L19, L22, L23, L24, L29, and L31e.
About this StructureAbout this Structure
1FG0 is a Single protein structure of sequence from Haloarcula marismortui. Full crystallographic information is available from OCA.
ReferenceReference
The structural basis of ribosome activity in peptide bond synthesis., Nissen P, Hansen J, Ban N, Moore PB, Steitz TA, Science. 2000 Aug 11;289(5481):920-30. PMID:10937990
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