2vt8

From Proteopedia

(Difference between revisions)

Current revision

Structure of a conserved dimerisation domain within Fbox7 and PI31

Structural highlights

2vt8 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PSMF1_HUMAN Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.^[1]

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

F-box proteins are the substrate-recognition components of the Skp1-Cul1-F box protein (SCF) E3 ubiquitin ligases. Here we report a structural relationship between Fbxo7, a component of the SCF(Fbxo7) E3 ligase, and the proteasome inhibitor PI31. SCF(Fbxo7) is known to catalyze the ubiquitination of hepatoma-up-regulated protein (HURP) and the inhibitor of apoptosis (IAP) protein but also functions as an activator of cyclin D-Cdk6 complexes. We identify PI31 as an Fbxo7.Skp1 binding partner and show that this interaction requires an N-terminal domain present in both proteins that we term the FP (Fbxo7/PI31) domain. The crystal structure of the PI31 FP domain reveals a novel alpha/beta-fold. Biophysical and mutational analyses are used to map regions of the PI31 FP domain mediating homodimerization and required for heterodimerization with Fbxo7.Skp1. Equivalent mutations in Fbxo7 ablate interaction with PI31 and also block Fbxo7 homodimerization. Knockdown of Fbxo7 does not affect PI31 levels arguing against PI31 being a substrate for SCF(Fbxo7). We present a model for FP domain-mediated dimerization of SCF(Fbxo7) and PI31.

Structure of a conserved dimerization domain within the F-box protein Fbxo7 and the PI31 proteasome inhibitor.,Kirk R, Laman H, Knowles PP, Murray-Rust J, Lomonosov M, Meziane el K, McDonald NQ J Biol Chem. 2008 Aug 8;283(32):22325-35. Epub 2008 May 20. PMID:18495667^[2]

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

References

↑ McCutchen-Maloney SL, Matsuda K, Shimbara N, Binns DD, Tanaka K, Slaughter CA, DeMartino GN. cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome. J Biol Chem. 2000 Jun 16;275(24):18557-65. PMID:10764772 doi:http://dx.doi.org/10.1074/jbc.M001697200
↑ Kirk R, Laman H, Knowles PP, Murray-Rust J, Lomonosov M, Meziane el K, McDonald NQ. Structure of a conserved dimerization domain within the F-box protein Fbxo7 and the PI31 proteasome inhibitor. J Biol Chem. 2008 Aug 8;283(32):22325-35. Epub 2008 May 20. PMID:18495667 doi:http://dx.doi.org/10.1074/jbc.M709900200

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/2vt8"

@@ Line 1: / Line 1: @@
 ==Structure of a conserved dimerisation domain within Fbox7 and PI31==
-<StructureSection load='2vt8' size='340' side='right' caption='[[2vt8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='2vt8' size='340' side='right'caption='[[2vt8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vt8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VT8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VT8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vt8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VT8 FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=2vt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vt8 OCA], [http://pdbe.org/2vt8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vt8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vt8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vt8 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vt8 OCA], [https://pdbe.org/2vt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vt8 RCSB], [https://www.ebi.ac.uk/pdbsum/2vt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vt8 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/PSMF1_HUMAN PSMF1_HUMAN] Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.<ref>PMID:10764772</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 12: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vt/2vt8_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Kirk, R J]]
+[[Category: Large Structures]]
-[[Category: Knowles, P P]]
+[[Category: Kirk RJ]]
-[[Category: Laman, H]]
+[[Category: Knowles PP]]
-[[Category: McDonald, N Q]]
+[[Category: Laman H]]
-[[Category: Murray-Rust, J]]
+[[Category: McDonald NQ]]
-[[Category: Hydrolase inhibitor]]
+[[Category: Murray-Rust J]]
-[[Category: Polymorphism]]

2vt8

From Proteopedia

Current revision

Structure of a conserved dimerisation domain within Fbox7 and PI31

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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