1914
From Proteopedia
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|PDB= 1914 |SIZE=350|CAPTION= <scene name='initialview01'>1914</scene>, resolution 2.53Å | |PDB= 1914 |SIZE=350|CAPTION= <scene name='initialview01'>1914</scene>, resolution 2.53Å | ||
|SITE= <scene name='pdbsite=NUL:Srp9/14+Complexed+w.+Alu+RNA+Forms+A+Distinct+Structural+...'>NUL</scene> | |SITE= <scene name='pdbsite=NUL:Srp9/14+Complexed+w.+Alu+RNA+Forms+A+Distinct+Structural+...'>NUL</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1914 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1914 OCA], [http://www.ebi.ac.uk/pdbsum/1914 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1914 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kapp, U.]] | [[Category: Kapp, U.]] | ||
[[Category: Strub, K.]] | [[Category: Strub, K.]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: PO4]] | ||
[[Category: alu domain]] | [[Category: alu domain]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
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[[Category: translation regulation]] | [[Category: translation regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:30:04 2008'' |
Revision as of 15:30, 30 March 2008
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| , resolution 2.53Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SIGNAL RECOGNITION PARTICLE ALU RNA BINDING HETERODIMER, SRP9/14
Overview
The mammalian signal recognition particle (SRP) is an 11S cytoplasmic ribonucleoprotein that plays an essential role in protein sorting. SRP recognizes the signal sequence of the nascent polypeptide chain emerging from the ribosome, and targets the ribosome-nascent chain-SRP complex to the rough endoplasmic reticulum. The SRP consists of six polypeptides (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) and a single 300 nucleotide RNA molecule. SRP9 and SRP14 proteins form a heterodimer that binds to the Alu domain of SRP RNA which is responsible for translation arrest. We report the first crystal structure of a mammalian SRP protein, that of the mouse SRP9/14 heterodimer, determined at 2.5 A resolution. SRP9 and SRP14 are found to be structurally homologous, containing the same alpha-beta-beta-beta-alpha fold. This we designate the Alu binding module (Alu bm), an additional member of the family of small alpha/beta RNA binding domains. The heterodimer has pseudo 2-fold symmetry and is saddle like, comprising a strongly curved six-stranded amphipathic beta-sheet with the four helices packed on the convex side and the exposed concave surface being lined with positively charged residues.
About this Structure
1914 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14., Birse DE, Kapp U, Strub K, Cusack S, Aberg A, EMBO J. 1997 Jul 1;16(13):3757-66. PMID:9233785
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