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1914

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Revision as of 09:21, 9 August 2017

SIGNAL RECOGNITION PARTICLE ALU RNA BINDING HETERODIMER, SRP9/14

Structural highlights

1914 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SRP14_MOUSE] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Birse DE, Kapp U, Strub K, Cusack S, Aberg A. The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14. EMBO J. 1997 Jul 1;16(13):3757-66. PMID:9233785 doi:10.1093/emboj/16.13.3757

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1914"

@@ Line 1: / Line 1: @@
 ==SIGNAL RECOGNITION PARTICLE ALU RNA BINDING HETERODIMER, SRP9/14==
 <StructureSection load='1914' size='340' side='right' caption='[[1914]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1914]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1914 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1914 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1914]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1914 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1914 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1914 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1914 RCSB], [http://www.ebi.ac.uk/pdbsum/1914 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1914 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1914 RCSB], [http://www.ebi.ac.uk/pdbsum/1914 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1914 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 24: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
 [[Category: Aberg, A]]
 [[Category: Birse, D]]

1914

From Proteopedia

Revision as of 09:21, 9 August 2017

SIGNAL RECOGNITION PARTICLE ALU RNA BINDING HETERODIMER, SRP9/14

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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