1dd5

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[[Image:1dd5.gif|left|200px]]
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{{Seed}}
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[[Image:1dd5.png|left|200px]]
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{{STRUCTURE_1dd5| PDB=1dd5 | SCENE= }}
{{STRUCTURE_1dd5| PDB=1dd5 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA RIBOSOME RECYCLING FACTOR, RRF'''
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===CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA RIBOSOME RECYCLING FACTOR, RRF===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10600747 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10600747}}
==About this Structure==
==About this Structure==
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[[Category: Beta-alpha-beta sandwich]]
[[Category: Beta-alpha-beta sandwich]]
[[Category: Three-helix bundle]]
[[Category: Three-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:42:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:50:54 2008''

Revision as of 19:50, 30 June 2008

Template:STRUCTURE 1dd5

CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA RIBOSOME RECYCLING FACTOR, RRF

Template:ABSTRACT PUBMED 10600747

About this Structure

1DD5 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic., Selmer M, Al-Karadaghi S, Hirokawa G, Kaji A, Liljas A, Science. 1999 Dec 17;286(5448):2349-52. PMID:10600747

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