5xgs

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Current revision (10:18, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5xgs' size='340' side='right'caption='[[5xgs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5xgs' size='340' side='right'caption='[[5xgs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xgs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XGS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XGS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xgs]] 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=5XGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XGS FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xgs OCA], [http://pdbe.org/5xgs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xgs RCSB], [http://www.ebi.ac.uk/pdbsum/5xgs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xgs ProSAT]</span></td></tr>
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</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&#8491;</td></tr>
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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=5xgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xgs OCA], [https://pdbe.org/5xgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xgs RCSB], [https://www.ebi.ac.uk/pdbsum/5xgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xgs ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/RCC1L_HUMAN RCC1L_HUMAN]] Williams syndrome. WBSCR16 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of WBSCR16 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.<ref>PMID:12073013</ref>
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[https://www.uniprot.org/uniprot/RCC1L_HUMAN RCC1L_HUMAN] Williams syndrome. WBSCR16 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of WBSCR16 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.<ref>PMID:12073013</ref>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/RCC1L_HUMAN RCC1L_HUMAN]
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WBSCR16 (Williams-Beuren Syndrome Chromosomal Region 16) gene is located in a large deletion region of Williams-Beuren syndrome (WBS), which is a neurodevelopmental disorder. Although the relationship between WBSCR16 and WBS remains unclear, it has been reported that WBSCR16 is a member of a functional module that regulates mitochondrial 16S rRNA abundance and intra-mitochondrial translation. WBSCR16 has RCC1 (Regulator of Chromosome Condensation 1)-like amino acid sequence repeats but the function of WBSCR16 appears to be different from that of other RCC1 superfamily members. Here, we demonstrate that WBSCR16 localizes to mitochondria in HeLa cells, and report the crystal structure of WBSCR16 determined to 2.0 A resolution using multi-wavelength anomalous diffraction. WBSCR16 adopts the seven-bladed beta-propeller fold characteristic of RCC1-like proteins. A comparison of the WBSCR16 structure with that of RCC1 and other RCC1-like proteins reveals that, although many of the residues buried in the core of the beta-propeller are highly conserved, the surface residues are poorly conserved and conformationally divergent.
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Crystal structure of human WBSCR16, an RCC1-like protein in mitochondria.,Koyama M, Sasaki T, Sasaki N, Matsuura Y Protein Sci. 2017 Jun 12. doi: 10.1002/pro.3210. PMID:28608466<ref>PMID:28608466</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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<div class="pdbe-citations 5xgs" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Koyama, M]]
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[[Category: Koyama M]]
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[[Category: Matsuura, Y]]
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[[Category: Matsuura Y]]
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[[Category: Sasaki, N]]
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[[Category: Sasaki N]]
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[[Category: Beta-propeller]]
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[[Category: Mitochondria]]
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[[Category: Rcc1-like protein]]
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[[Category: Unknown function]]
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Current revision

Crystal structure of human WBSCR16

PDB ID 5xgs

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