6lag

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Current revision (10:54, 14 June 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6lag is ON HOLD until Paper Publication
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==Solution structure of SPA-2 SHD==
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<StructureSection load='6lag' size='340' side='right'caption='[[6lag]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6lag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LAG FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6lag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lag OCA], [https://pdbe.org/6lag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lag RCSB], [https://www.ebi.ac.uk/pdbsum/6lag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lag ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/V5IQM7_NEUCR V5IQM7_NEUCR]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Spitzenkorper (SPK) constitutes a collection of secretory vesicles and polarity-related proteins intimately associated with polarized growth of fungal hyphae. Many SPK-localized proteins are known, but their assembly and dynamics remain poorly understood. Here, we identify protein-protein interaction cascades leading to assembly of two SPK scaffolds and recruitment of diverse effectors in Neurospora crassa. Both scaffolds are transported to the SPK by the myosin V motor (MYO-5), with the coiled-coil protein SPZ-1 acting as cargo adaptor. Neither scaffold appears to be required for accumulation of SPK secretory vesicles. One scaffold consists of Leashin-2 (LAH-2), which is required for SPK localization of the signalling kinase COT-1 and the glycolysis enzyme GPI-1. The other scaffold comprises a complex of Janus-1 (JNS-1) and the polarisome protein SPA-2. Via its Spa homology domain (SHD), SPA-2 recruits a calponin domain-containing F-actin effector (CCP-1). The SHD NMR structure reveals a conserved surface groove required for effector binding. Similarities between SPA-2/JNS-1 and the metazoan GIT/PIX complex identify foundational features of the cell polarity apparatus that predate the fungal-metazoan divergence.
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Authors: Fan, J.S., Wong, J.Y., Zheng, P., Yang, D., Jedd, G.
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Spitzenkorper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds.,Zheng P, Nguyen TA, Wong JY, Lee M, Nguyen TA, Fan JS, Yang D, Jedd G Nat Commun. 2020 Jun 5;11(1):2830. doi: 10.1038/s41467-020-16712-9. PMID:32503980<ref>PMID:32503980</ref>
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Description: Solution structure of SPA-2 SHD
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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: Yang, D]]
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<div class="pdbe-citations 6lag" style="background-color:#fffaf0;"></div>
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[[Category: Zheng, P]]
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== References ==
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[[Category: Jedd, G]]
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<references/>
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[[Category: Fan, J.S]]
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__TOC__
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[[Category: Wong, J.Y]]
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Neurospora crassa]]
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[[Category: Fan JS]]
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[[Category: Jedd G]]
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[[Category: Wong JY]]
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[[Category: Yang D]]
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[[Category: Zheng P]]

Current revision

Solution structure of SPA-2 SHD

PDB ID 6lag

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