364d
From Proteopedia
(New page: 200px<br /><applet load="364d" size="450" color="white" frame="true" align="right" spinBox="true" caption="364d, resolution 3.000Å" /> '''3.0 A STRUCTURE OF ...) |
|||
Line 1: | Line 1: | ||
- | [[Image:364d.jpg|left|200px]]<br /><applet load="364d" size=" | + | [[Image:364d.jpg|left|200px]]<br /><applet load="364d" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="364d, resolution 3.000Å" /> | caption="364d, resolution 3.000Å" /> | ||
'''3.0 A STRUCTURE OF FRAGMENT I FROM E. COLI 5S RRNA'''<br /> | '''3.0 A STRUCTURE OF FRAGMENT I FROM E. COLI 5S RRNA'''<br /> | ||
==Overview== | ==Overview== | ||
- | Two new RNA structures portray how non-Watson-Crick base pairs and metal | + | Two new RNA structures portray how non-Watson-Crick base pairs and metal ions can produce a unique RNA shape suitable for recognition by proteins. The crystal structures of a 62 nt domain of E. coli 5S ribosomal RNA and a duplex dodecamer encompassing an internal loop E have been determined at 3.0 and 1.5 A, respectively. This loop E region is distorted by three "cross-strand purine stacks" and three novel, water-mediated noncanonical base pairs and stabilized by a four metal ion zipper. These features give its minor groove a unique hydrogen-bonding surface and make the adjacent major groove wide enough to permit recognition by the ribosomal protein L25, which is expected to bind to this surface. |
==About this Structure== | ==About this Structure== | ||
- | 364D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 364D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 356D. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=364D OCA]. |
==Reference== | ==Reference== | ||
Line 13: | Line 13: | ||
[[Category: ]] | [[Category: ]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
- | [[Category: Correll, C | + | [[Category: Correll, C C.]] |
[[Category: Freeborn, B.]] | [[Category: Freeborn, B.]] | ||
- | [[Category: Moore, P | + | [[Category: Moore, P B.]] |
- | [[Category: Steitz, T | + | [[Category: Steitz, T A.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: double helix]] | [[Category: double helix]] | ||
Line 26: | Line 26: | ||
[[Category: u-rna]] | [[Category: u-rna]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:02:21 2008'' |
Revision as of 17:02, 21 February 2008
|
3.0 A STRUCTURE OF FRAGMENT I FROM E. COLI 5S RRNA
Overview
Two new RNA structures portray how non-Watson-Crick base pairs and metal ions can produce a unique RNA shape suitable for recognition by proteins. The crystal structures of a 62 nt domain of E. coli 5S ribosomal RNA and a duplex dodecamer encompassing an internal loop E have been determined at 3.0 and 1.5 A, respectively. This loop E region is distorted by three "cross-strand purine stacks" and three novel, water-mediated noncanonical base pairs and stabilized by a four metal ion zipper. These features give its minor groove a unique hydrogen-bonding surface and make the adjacent major groove wide enough to permit recognition by the ribosomal protein L25, which is expected to bind to this surface.
About this Structure
364D is a Protein complex structure of sequences from [1] with as ligand. This structure supersedes the now removed PDB entry 356D. Full crystallographic information is available from OCA.
Reference
Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain., Correll CC, Freeborn B, Moore PB, Steitz TA, Cell. 1997 Nov 28;91(5):705-12. PMID:9393863 [[Category: ]]
Page seeded by OCA on Thu Feb 21 19:02:21 2008
Categories: Protein complex | Correll, C C. | Freeborn, B. | Moore, P B. | Steitz, T A. | MG | Double helix | Internal loop | Kinked | Mismatched | Modified | Overhanging base | U-rna