1c04: Difference between revisions
New page: left|200px<br /><applet load="1c04" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c04, resolution 5.0Å" /> '''IDENTIFICATION OF KNO... |
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[[Image:1c04.gif|left|200px]]<br /><applet load="1c04" size=" | [[Image:1c04.gif|left|200px]]<br /><applet load="1c04" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1c04, resolution 5.0Å" /> | caption="1c04, resolution 5.0Å" /> | ||
'''IDENTIFICATION OF KNOWN PROTEIN AND RNA STRUCTURES IN A 5 A MAP OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI'''<br /> | '''IDENTIFICATION OF KNOWN PROTEIN AND RNA STRUCTURES IN A 5 A MAP OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI'''<br /> | ||
==Overview== | ==Overview== | ||
We have calculated at 5.0 A resolution an electron-density map of the | We have calculated at 5.0 A resolution an electron-density map of the large 50S ribosomal subunit from the bacterium Haloarcula marismortui by using phases derived from four heavy-atom derivatives, intercrystal density averaging and density-modification procedures. More than 300 base pairs of A-form RNA duplex have been fitted into this map, as have regions of non-A-form duplex, single-stranded segments and tetraloops. The long rods of RNA crisscrossing the subunit arise from the stacking of short, separate double helices, not all of which are A-form, and in many places proteins crosslink two or more of these rods. The polypeptide exit channel was marked by tungsten cluster compounds bound in one heavy-atom-derivatized crystal. We have determined the structure of the translation-factor-binding centre by fitting the crystal structures of the ribosomal proteins L6, L11 and L14, the sarcin-ricin loop RNA, and the RNA sequence that binds L11 into the electron density. We can position either elongation factor G or elongation factor Tu complexed with an aminoacylated transfer RNA and GTP onto the factor-binding centre in a manner that is consistent with results from biochemical and electron microscopy studies. | ||
==About this Structure== | ==About this Structure== | ||
1C04 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http:// | 1C04 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1C04 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Ban, N.]] | [[Category: Ban, N.]] | ||
[[Category: Capel, M.]] | [[Category: Capel, M.]] | ||
[[Category: Moore, P | [[Category: Moore, P B.]] | ||
[[Category: Nissen, P.]] | [[Category: Nissen, P.]] | ||
[[Category: Steitz, T | [[Category: Steitz, T A.]] | ||
[[Category: large ribosome unit]] | [[Category: large ribosome unit]] | ||
[[Category: low resolution model]] | [[Category: low resolution model]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:04 2008'' | ||
Revision as of 10:01, 21 February 2008
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IDENTIFICATION OF KNOWN PROTEIN AND RNA STRUCTURES IN A 5 A MAP OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI
Overview
We have calculated at 5.0 A resolution an electron-density map of the large 50S ribosomal subunit from the bacterium Haloarcula marismortui by using phases derived from four heavy-atom derivatives, intercrystal density averaging and density-modification procedures. More than 300 base pairs of A-form RNA duplex have been fitted into this map, as have regions of non-A-form duplex, single-stranded segments and tetraloops. The long rods of RNA crisscrossing the subunit arise from the stacking of short, separate double helices, not all of which are A-form, and in many places proteins crosslink two or more of these rods. The polypeptide exit channel was marked by tungsten cluster compounds bound in one heavy-atom-derivatized crystal. We have determined the structure of the translation-factor-binding centre by fitting the crystal structures of the ribosomal proteins L6, L11 and L14, the sarcin-ricin loop RNA, and the RNA sequence that binds L11 into the electron density. We can position either elongation factor G or elongation factor Tu complexed with an aminoacylated transfer RNA and GTP onto the factor-binding centre in a manner that is consistent with results from biochemical and electron microscopy studies.
About this Structure
1C04 is a Protein complex structure of sequences from Haloarcula marismortui. Full crystallographic information is available from OCA.
Reference
Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit., Ban N, Nissen P, Hansen J, Capel M, Moore PB, Steitz TA, Nature. 1999 Aug 26;400(6747):841-7. PMID:10476961
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