2jun

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[[Image:2jun.jpg|left|200px]]
 
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{{Structure
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==Structure of the MID1 tandem B-boxes reveals an interaction reminiscent of intermolecular RING heterodimers==
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|PDB= 2jun |SIZE=350|CAPTION= <scene name='initialview01'>2jun</scene>
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<StructureSection load='2jun' size='340' side='right'caption='[[2jun]]' scene=''>
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|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+220'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A+221'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+A+222'>AC3</scene> and <scene name='pdbsite=AC4:Zn+Binding+Site+For+Residue+A+223'>AC4</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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<table><tr><td colspan='2'>[[2jun]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JUN FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= MID1, FXY, RNF59, TRIM18, XPRF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jun OCA], [https://pdbe.org/2jun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jun RCSB], [https://www.ebi.ac.uk/pdbsum/2jun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jun ProSAT]</span></td></tr>
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</table>
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'''Structure of the MID1 tandem B-boxes reveals an interaction reminiscent of intermolecular RING heterodimers'''
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== Disease ==
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[https://www.uniprot.org/uniprot/TRI18_HUMAN TRI18_HUMAN] Defects in MID1 are the cause of Opitz GBBB syndrome 1 (OGS1) [MIM:[https://omim.org/entry/300000 300000]. A congenital midline malformation syndrome characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. Note=MID1 mutations produce proteins with a decreased affinity for microtubules.<ref>PMID:9354791</ref> <ref>PMID:11030761</ref> <ref>PMID:9718340</ref> <ref>PMID:15558842</ref>
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== Function ==
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==Overview==
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[https://www.uniprot.org/uniprot/TRI18_HUMAN TRI18_HUMAN] Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination.<ref>PMID:10400985</ref> <ref>PMID:11685209</ref> <ref>PMID:22613722</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ju/2jun_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2jun ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The tripartite motif (TRIM) protein family, defined by N-terminal RING, B-box, and coiled-coil (RBCC) domains, consists of either a single type 2 B-box domain or tandem B-box domains of type 1 and type 2 (B1B2). Here, we report the first structure of the B-box domains in their native tandem orientation. The B-boxes are from Midline-1, a putative ubiquitin E3 ligase that is required for the proteosomal degradation of the catalytic subunit of protein phosphatase 2A (PP2Ac). This function of MID1 is facilitated by the direct binding of Alpha4, a regulatory subunit of PP2Ac, to B-box1, while B-box2 appears to influence this interaction. Both B-box1 and B-box2 bind two zinc atoms in a cross-brace motif and adopt a similar betabetaalpha structure reminiscent of the RING, PHD, ZZ, and U-box domains, although they differ from each other and with RING domains in the spacing of their zinc-binding residues. The two B-box domains pack against each other with the interface formed by residues located on the structured loop consisting of the two antiparallel beta-strands. The surface area of the interface is 188 A2 (17% of the total surface). Consistent with the globular structure, the Tm of the tandem B-box domain (59 degrees C) is higher than the individual domains, supporting a stable interaction between the B-box 1 and 2 domains. Notably, the interaction is reminiscent of the interaction of recently determined RING dimers, suggesting the possibility of an evolutionarily conserved role for B-box2 domains in regulating functional RING-type folds.
The tripartite motif (TRIM) protein family, defined by N-terminal RING, B-box, and coiled-coil (RBCC) domains, consists of either a single type 2 B-box domain or tandem B-box domains of type 1 and type 2 (B1B2). Here, we report the first structure of the B-box domains in their native tandem orientation. The B-boxes are from Midline-1, a putative ubiquitin E3 ligase that is required for the proteosomal degradation of the catalytic subunit of protein phosphatase 2A (PP2Ac). This function of MID1 is facilitated by the direct binding of Alpha4, a regulatory subunit of PP2Ac, to B-box1, while B-box2 appears to influence this interaction. Both B-box1 and B-box2 bind two zinc atoms in a cross-brace motif and adopt a similar betabetaalpha structure reminiscent of the RING, PHD, ZZ, and U-box domains, although they differ from each other and with RING domains in the spacing of their zinc-binding residues. The two B-box domains pack against each other with the interface formed by residues located on the structured loop consisting of the two antiparallel beta-strands. The surface area of the interface is 188 A2 (17% of the total surface). Consistent with the globular structure, the Tm of the tandem B-box domain (59 degrees C) is higher than the individual domains, supporting a stable interaction between the B-box 1 and 2 domains. Notably, the interaction is reminiscent of the interaction of recently determined RING dimers, suggesting the possibility of an evolutionarily conserved role for B-box2 domains in regulating functional RING-type folds.
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==About this Structure==
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Structure of the MID1 Tandem B-Boxes Reveals an Interaction Reminiscent of Intermolecular Ring Heterodimers(,).,Tao H, Simmons BN, Singireddy S, Jakkidi M, Short KM, Cox TC, Massiah MA Biochemistry. 2008 Feb 26;47(8):2450-2457. Epub 2008 Jan 26. PMID:18220417<ref>PMID:18220417</ref>
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2JUN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JUN OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of the MID1 Tandem B-Boxes Reveals an Interaction Reminiscent of Intermolecular Ring Heterodimers(,)., Tao H, Simmons BN, Singireddy S, Jakkidi M, Short KM, Cox TC, Massiah MA, Biochemistry. 2008 Feb 26;47(8):2450-2457. Epub 2008 Jan 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18220417 18220417]
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</div>
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<div class="pdbe-citations 2jun" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cox, T C.]]
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[[Category: Cox TC]]
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[[Category: Jakkidi, M.]]
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[[Category: Jakkidi M]]
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[[Category: Massiah, M A.]]
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[[Category: Massiah MA]]
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[[Category: Short, K M.]]
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[[Category: Short KM]]
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[[Category: Simmons, B N.]]
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[[Category: Simmons BN]]
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[[Category: Singireddy, S.]]
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[[Category: Singireddy S]]
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[[Category: Tao, H.]]
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[[Category: Tao H]]
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[[Category: ZN]]
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[[Category: alternative splicing]]
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[[Category: b-box]]
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[[Category: coiled coil]]
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[[Category: cytoplasm]]
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[[Category: cytoskeleton]]
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[[Category: disease mutation]]
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[[Category: ligase]]
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[[Category: metal-binding]]
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[[Category: microtubule]]
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[[Category: midline 1]]
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[[Category: phosphorylation]]
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[[Category: ring finger]]
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[[Category: trim]]
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[[Category: ubl conjugation pathway]]
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[[Category: zinc]]
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[[Category: zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:45:13 2008''
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Current revision

Structure of the MID1 tandem B-boxes reveals an interaction reminiscent of intermolecular RING heterodimers

PDB ID 2jun

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