3ff5

From Proteopedia

(Difference between revisions)

Revision as of 21:03, 7 February 2016

Crystal structure of the conserved N-terminal domain of the peroxisomal matrix-protein-import receptor, Pex14p

Structural highlights

3ff5 is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	Pex14 (Buffalo rat)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PEX14_RAT] Peroxisome membrane protein that is an essential component of the peroxisomal import machinery. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PEX5). Plays a key role for peroxisome movement through a direct interaction with tubulin.[UniProtKB:O75381]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Pex14p is a central component of the peroxisomal protein import machinery, in which the conserved N-terminal domain mediates dynamic interactions with other peroxins including Pex5p, Pex13p, and Pex19p. Here, we report the crystal structure of the conserved N-terminal domain of Pex14p with a three-helix bundle. A hydrophobic surface is composed of the conserved residues, of which two phenylalanine residues (Phe-35 and Phe-52) protrude to the solvent. Consequently, two putative binding pockets suitable for recognizing the helical WXXXF/Y motif of Pex5p are formed on the surface by the two phenylalanine residues accompanying with positively charged residues. The structural feature agrees well with our earlier findings where F35A/L36A and F52A/L53A mutants were impaired in the interactions with other peroxins such as Pex5p and Pex13p. Pex14p variants each with Phe-to-Ala mutation at positions 35, 52, and 35/52, respectively, were defective in restoring the impaired peroxisomal protein import in pex14 Chinese hamster ovary mutant ZP161 cells. Moreover, in GST pull-down assays His(6)-Pex5pL bound only to GST-Pex14p(25-70), not to any of GST-Pex14p(25-70)F35A, GST-Pex14p(25-70)F52A, and GST-Pex14p(25-70)F35A/F52A. Endogenous Pex5p was recruited to FLAG-Pex14p on peroxisomes in vivo but barely to FLAG-Pex14pF35A, FLAG-Pex14pF52A, and FLAG-Pex14pF35A/F52A. Collectively, Phe-35 and Phe-52 are essential for the Pex14p functions, including the interaction between Pex14p and Pex5p.

Crystal structure of the conserved N-terminal domain of the peroxisomal matrix protein import receptor, Pex14p.,Su JR, Takeda K, Tamura S, Fujiki Y, Miki K Proc Natl Acad Sci U S A. 2009 Jan 13;106(2):417-21. Epub 2009 Jan 2. PMID:19122147^[1]

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

References

↑ Su JR, Takeda K, Tamura S, Fujiki Y, Miki K. Crystal structure of the conserved N-terminal domain of the peroxisomal matrix protein import receptor, Pex14p. Proc Natl Acad Sci U S A. 2009 Jan 13;106(2):417-21. Epub 2009 Jan 2. PMID:19122147 doi:10.1073/pnas.0808681106

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ff5"

@@ Line 2: / Line 2: @@
 <StructureSection load='3ff5' size='340' side='right' caption='[[3ff5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ff5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FF5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ff5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FF5 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPW:DECYL+2-TRIMETHYLAZANIUMYLETHYL+PHOSPHATE'>DPW</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pex14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pex14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3ff5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ff5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ff5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ff5 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=3ff5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ff5 OCA], [http://pdbe.org/3ff5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ff5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ff5 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PEX14_RAT PEX14_RAT]] Peroxisome membrane protein that is an essential component of the peroxisomal import machinery. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PEX5). Plays a key role for peroxisome movement through a direct interaction with tubulin.[UniProtKB:O75381]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 15: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ff5 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3ff5" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Rattus norvegicus]]
+[[Category: Buffalo rat]]
 [[Category: Fujiki, Y]]
 [[Category: Miki, K]]

3ff5

From Proteopedia

Revision as of 21:03, 7 February 2016

Crystal structure of the conserved N-terminal domain of the peroxisomal matrix-protein-import receptor, Pex14p

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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