5ghu

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'''Unreleased structure'''
 
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The entry 5ghu is ON HOLD until sometime in the future
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==Crystal structure of YadV chaperone at 1.63 Angstrom==
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<StructureSection load='5ghu' size='340' side='right'caption='[[5ghu]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ghu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GHU 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]] 1.63&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=5ghu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ghu OCA], [https://pdbe.org/5ghu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ghu RCSB], [https://www.ebi.ac.uk/pdbsum/5ghu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ghu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/YADV_ECOLI YADV_ECOLI] Part of the yadCKLM-htrE-yadVN fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches.<ref>PMID:20345943</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cell surface pili assembled by the chaperone-usher (CU) pathway play a crucial role in the adhesion of uropathogenic Escherichia coli. YadV is the chaperone component of the CU pathway of Yad pili. Here, we report the crystal structure of YadV from E. coli. In contrast to major usher chaperones, YadV is a monomer in solution as well as in the crystallographic symmetry, and the monomeric form is a preferred state for interacting with pilus subunits. Moreover, we observed a closed conformation for the proline lock, a crucial structural element for chaperone-pilus subunit interaction. MD simulation shows that the closed state of the proline lock is not energetically stable. Thus, the structure of monomeric YadV with its closed proline lock may serve as an intermediate state to provide suitable access to pilus subunits.
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Authors: Pandey, N.K., Bhavesh, N.S.
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Crystal structure of the usher chaperone YadV reveals a monomer with the proline lock in closed conformation suggestive of an intermediate state.,Pandey NK, Verma G, Kushwaha GS, Suar M, Bhavesh NS FEBS Lett. 2020 Jul 10. doi: 10.1002/1873-3468.13883. PMID:32649775<ref>PMID:32649775</ref>
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Description: Crystal structure of EcpD chaperone at 1.63 Angstrom
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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: Pandey, N.K]]
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<div class="pdbe-citations 5ghu" style="background-color:#fffaf0;"></div>
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[[Category: Bhavesh, N.S]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Bhavesh NS]]
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[[Category: Pandey NK]]

Current revision

Crystal structure of YadV chaperone at 1.63 Angstrom

PDB ID 5ghu

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