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5bmy

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(New page: '''Unreleased structure''' The entry 5bmy is ON HOLD Authors: Hanazono, Y., Takeda, K., Miki, K. Description: Crystal structure of hPin1 WW domain (5-22) fused with maltose-binding pro...)
Current revision (16:04, 8 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5bmy is ON HOLD
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==Crystal structure of hPin1 WW domain (5-21) fused with maltose-binding protein==
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<StructureSection load='5bmy' size='340' side='right'caption='[[5bmy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5bmy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BMY 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">X-ray diffraction, [[Resolution|Resolution]] 2.001&#8491;</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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></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=5bmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bmy OCA], [https://pdbe.org/5bmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bmy RCSB], [https://www.ebi.ac.uk/pdbsum/5bmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bmy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.<ref>PMID:15664191</ref> <ref>PMID:16644721</ref> <ref>PMID:21497122</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Nascent proteins fold co-translationally because the folding speed and folding pathways are limited by the rate of ribosome biosynthesis in the living cell. In addition, though full-length proteins can fold all their residues during the folding process, nascent proteins initially fold only with the N-terminal residues. However, the transient structure and the co-translational folding pathway are not well understood. Here we report the atomic structures of a series of N-terminal fragments of the WW domain with increasing amino acid length. Unexpectedly, the structures indicate that the intermediate-length fragments take helical conformations even though the full-length protein has no helical regions. The circular dichroism spectra and theoretical calculations also support the crystallographic results. This suggests that the short-range interactions are more decisive in the structure formation than the long-range interactions for short nascent proteins. In the course of the peptide extension, the helical structure change to the structure mediated by the long-range interactions at a particular polypeptide length. Our results will provide unique information for elucidating the nature of co-translational folding.
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Authors: Hanazono, Y., Takeda, K., Miki, K.
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Structural studies of the N-terminal fragments of the WW domain: Insights into co-translational folding of a beta-sheet protein.,Hanazono Y, Takeda K, Miki K Sci Rep. 2016 Oct 4;6:34654. doi: 10.1038/srep34654. PMID:27698466<ref>PMID:27698466</ref>
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Description: Crystal structure of hPin1 WW domain (5-22) fused with maltose-binding protein
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Takeda, K]]
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<div class="pdbe-citations 5bmy" style="background-color:#fffaf0;"></div>
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[[Category: Hanazono, Y]]
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== References ==
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[[Category: Miki, K]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli O157:H7]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Hanazono Y]]
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[[Category: Miki K]]
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[[Category: Takeda K]]

Current revision

Crystal structure of hPin1 WW domain (5-21) fused with maltose-binding protein

PDB ID 5bmy

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