1dd5: Difference between revisions

Line 1:

[[Image:1dd5.gif|left|200px]]<br /><applet load="1dd5" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1dd5.gif|left|200px]]<br /><applet load="1dd5" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1dd5, resolution 2.55Å" />

'''CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA RIBOSOME RECYCLING FACTOR, RRF'''<br />

==Overview==

Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The, crystal structure of RRF was determined at 2.55 angstrom resolution. The, protein has an unusual fold where domain I is a long three-helix bundle, and domain II is a three-layer beta/alpha/beta sandwich. The molecule, superimposes almost perfectly with a transfer RNA (tRNA) except that the, amino acid-binding 3' end is missing. The mimicry suggests that RRF, interacts with the posttermination ribosomal complex in a similar manner, to a tRNA, leading to disassembly of the complex. The structural, arrangement of this mimicry is entirely different from that of other cases, of less pronounced mimicry of tRNA so far described.

Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The crystal structure of RRF was determined at 2.55 angstrom resolution. The protein has an unusual fold where domain I is a long three-helix bundle and domain II is a three-layer beta/alpha/beta sandwich. The molecule superimposes almost perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3' end is missing. The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex. The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so far described.

==About this Structure==

1DD5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1DD5 OCA].

1DD5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD5 OCA].

==Reference==

Line 22:

[[Category: three-helix bundle]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 13~~:11:~~10 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:29 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1dd5.gif|left|200px]]<br /><applet load="1dd5" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dd5.gif|left|200px]]<br /><applet load="1dd5" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dd5, resolution 2.55&Aring;" />
 '''CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA RIBOSOME RECYCLING FACTOR, RRF'''<br />
 ==Overview==
-Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The, crystal structure of RRF was determined at 2.55 angstrom resolution. The, protein has an unusual fold where domain I is a long three-helix bundle, and domain II is a three-layer beta/alpha/beta sandwich. The molecule, superimposes almost perfectly with a transfer RNA (tRNA) except that the, amino acid-binding 3' end is missing. The mimicry suggests that RRF, interacts with the posttermination ribosomal complex in a similar manner, to a tRNA, leading to disassembly of the complex. The structural, arrangement of this mimicry is entirely different from that of other cases, of less pronounced mimicry of tRNA so far described.
+Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The crystal structure of RRF was determined at 2.55 angstrom resolution. The protein has an unusual fold where domain I is a long three-helix bundle and domain II is a three-layer beta/alpha/beta sandwich. The molecule superimposes almost perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3' end is missing. The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex. The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so far described.
 ==About this Structure==
-DD5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DD5 OCA].
+DD5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD5 OCA].
 ==Reference==
@@ Line 22: / Line 22: @@
 [[Category: three-helix bundle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:11:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:29 2008''