2dq5

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{{Seed}}
 
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[[Image:2dq5.png|left|200px]]
 
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==solution structure of the Mid1 B Box2 Chc(D/C)C2H2 Zinc-Binding Domain: insights into an evolutionary conserved ring fold==
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The line below this paragraph, containing "STRUCTURE_2dq5", creates the "Structure Box" on the page.
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<StructureSection load='2dq5' size='340' side='right'caption='[[2dq5]]' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2dq5]] 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=2DQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DQ5 FirstGlance]. <br>
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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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<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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{{STRUCTURE_2dq5| PDB=2dq5 | SCENE= }}
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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=2dq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dq5 OCA], [https://pdbe.org/2dq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dq5 RCSB], [https://www.ebi.ac.uk/pdbsum/2dq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dq5 ProSAT]</span></td></tr>
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</table>
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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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[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/dq/2dq5_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=2dq5 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 ==
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The B-box type 2 domain is a prominent feature of a large and growing family of RING, B-box, coiled-coil (RBCC) domain-containing proteins and is also present in more than 1500 additional proteins. Most proteins usually contain a single B-box2 domain, although some proteins contain tandem domains consisting of both type 1 and type 2 B-boxes, which actually share little sequence similarity. Recently, we determined the solution structure of B-box1 from MID1, a putative E3 ubiquitin ligase that is mutated in X-linked Opitz G/BBB syndrome, and showed that it adopted a betabetaalpha RING-like fold. Here, we report the tertiary structure of the B-box2 (CHC(D/C)C(2)H(2)) domain from MID1 using multidimensional NMR spectroscopy. This MID1 B-box2 domain consists of a short alpha-helix and a structured loop with two short anti-parallel beta-strands and adopts a tertiary structure similar to the B-box1 and RING structures, even though there is minimal primary sequence similarity between these domains. By mutagenesis, ESI-FTICR and ICP mass spectrometry, we show that the B-box2 domain coordinates two zinc atoms with a 'cross-brace' pattern: one by Cys175, His178, Cys195 and Cys198 and the other by Cys187, Asp190, His204, and His207. Interestingly, this is the first case that an aspartic acid is involved in zinc atom coordination in a zinc-finger domain, although aspartic acid has been shown to coordinate non-catalytic zinc in matrix metalloproteinases. In addition, the finding of a Cys195Phe substitution identified in a patient with X-linked Opitz GBBB syndrome supports the importance of proper zinc coordination for the function of the MID1 B-box2 domain. Notably, however, our structure differs from the only other published B-box2 structure, that from XNF7, which was shown to coordinate one zinc atom. Finally, the similarity in tertiary structures of the B-box2, B-box1 and RING domains suggests these domains have evolved from a common ancestor.
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===solution structure of the Mid1 B Box2 Chc(D/C)C2H2 Zinc-Binding Domain: insights into an evolutionary conserved ring fold===
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Solution structure of the MID1 B-box2 CHC(D/C)C(2)H(2) zinc-binding domain: insights into an evolutionarily conserved RING fold.,Massiah MA, Matts JA, Short KM, Simmons BN, Singireddy S, Yi Z, Cox TC J Mol Biol. 2007 May 25;369(1):1-10. Epub 2007 Mar 15. PMID:17428496<ref>PMID:17428496</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17428496}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2dq5" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17428496 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17428496}}
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__TOC__
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Opitz G syndrome, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300552 300552]]
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==About this Structure==
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2DQ5 is a 1 chain 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=2DQ5 OCA].
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==Reference==
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<ref group="xtra">PMID:17428496</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Cox, T C.]]
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[[Category: Large Structures]]
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[[Category: Massiah, M A.]]
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[[Category: Cox TC]]
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[[Category: Matts, J A.B.]]
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[[Category: Massiah MA]]
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[[Category: Short, K M.]]
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[[Category: Matts JAB]]
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[[Category: Simmons, B N.]]
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[[Category: Short KM]]
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[[Category: Singireddy, S.]]
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[[Category: Simmons BN]]
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[[Category: Zou, J.]]
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[[Category: Singireddy S]]
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[[Category: E3 ligase]]
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[[Category: Zou J]]
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[[Category: Ring like]]
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[[Category: Zinc coordination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 19 08:38:31 2009''
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Current revision

solution structure of the Mid1 B Box2 Chc(D/C)C2H2 Zinc-Binding Domain: insights into an evolutionary conserved ring fold

PDB ID 2dq5

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