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8hbr

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'''Unreleased structure'''
 
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The entry 8hbr is ON HOLD
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==The C-terminal domain of Spiral2==
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<StructureSection load='8hbr' size='340' side='right'caption='[[8hbr]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8hbr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Physcomitrium_patens Physcomitrium patens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HBR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=8hbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hbr OCA], [https://pdbe.org/8hbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hbr RCSB], [https://www.ebi.ac.uk/pdbsum/8hbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hbr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A2K1IUB4_PHYPA A0A2K1IUB4_PHYPA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Plant cells form microtubule arrays, called ;cortical microtubules', beneath the plasma membrane which are critical for cell-wall organization and directional cell growth. Cortical microtubules are nucleated independently of centrosomes. Spiral2 is a land-plant-specific microtubule minus-end-targeting protein that stabilizes the minus ends by inhibiting depolymerization of the filament. Spiral2 possesses an N-terminal microtubule-binding domain and a conserved C-terminal domain whose function is unknown. In this study, the crystal structure of the conserved C-terminal domain of Spiral2 was determined using the single-wavelength anomalous dispersion method. Refinement of the model to a resolution of 2.2 A revealed a helix-turn-helix fold with seven alpha-helices. The protein crystallized as a dimer, but SEC-MALS analysis showed the protein to be monomeric. A structural homology search revealed that the protein has similarity to the C-terminal domain of the katanin regulatory subunit p80. The structure presented here suggests that the C-terminal domain of Spiral2 represents a new class of microtubule dynamics modulator across the kingdom.
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Authors:
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Crystal structure of the C-terminal domain of the plant-specific microtubule-associated protein Spiral2.,Ohno M, Higuchi Y, Hayashi I Acta Crystallogr F Struct Biol Commun. 2023 Jan 1;79(Pt 1):17-22. doi: , 10.1107/S2053230X22011815. Epub 2023 Jan 1. PMID:36598352<ref>PMID:36598352</ref>
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Description:
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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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<div class="pdbe-citations 8hbr" style="background-color:#fffaf0;"></div>
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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: Large Structures]]
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[[Category: Physcomitrium patens]]
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[[Category: Hayashi I]]

Current revision

The C-terminal domain of Spiral2

PDB ID 8hbr

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