3b9p

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[[Image:3b9p.jpg|left|200px]]
 
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{{Structure
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==Spastin==
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|PDB= 3b9p |SIZE=350|CAPTION= <scene name='initialview01'>3b9p</scene>, resolution 2.70&Aring;
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<StructureSection load='3b9p' size='340' side='right'caption='[[3b9p]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Residue+A+19'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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<table><tr><td colspan='2'>[[3b9p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B9P FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.7&#8491;</td></tr>
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|GENE= spas ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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|DOMAIN=
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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=3b9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9p OCA], [https://pdbe.org/3b9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b9p RCSB], [https://www.ebi.ac.uk/pdbsum/3b9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b9p ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9p OCA], [http://www.ebi.ac.uk/pdbsum/3b9p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b9p RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/SPAST_DROME SPAST_DROME] ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse.<ref>PMID:15242610</ref> <ref>PMID:15562320</ref> <ref>PMID:15823537</ref> <ref>PMID:16276413</ref> <ref>PMID:17452528</ref> <ref>PMID:19341724</ref> <ref>PMID:18202664</ref>
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== Evolutionary Conservation ==
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'''Spastin'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b9/3b9p_consurf.spt"</scriptWhenChecked>
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Spastin, the most common locus for mutations in hereditary spastic paraplegias, and katanin are related microtubule-severing AAA ATPases involved in constructing neuronal and non-centrosomal microtubule arrays and in segregating chromosomes. The mechanism by which spastin and katanin break and destabilize microtubules is unknown, in part owing to the lack of structural information on these enzymes. Here we report the X-ray crystal structure of the Drosophila spastin AAA domain and provide a model for the active spastin hexamer generated using small-angle X-ray scattering combined with atomic docking. The spastin hexamer forms a ring with a prominent central pore and six radiating arms that may dock onto the microtubule. Helices unique to the microtubule-severing AAA ATPases surround the entrances to the pore on either side of the ring, and three highly conserved loops line the pore lumen. Mutagenesis reveals essential roles for these structural elements in the severing reaction. Peptide and antibody inhibition experiments further show that spastin may dismantle microtubules by recognizing specific features in the carboxy-terminal tail of tubulin. Collectively, our data support a model in which spastin pulls the C terminus of tubulin through its central pore, generating a mechanical force that destabilizes tubulin-tubulin interactions within the microtubule lattice. Our work also provides insights into the structural defects in spastin that arise from mutations identified in hereditary spastic paraplegia patients.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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3B9P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B9P OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3b9p ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin., Roll-Mecak A, Vale RD, Nature. 2008 Jan 17;451(7176):363-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18202664 18202664]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Roll-Mecak, A.]]
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[[Category: Roll-Mecak A]]
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[[Category: Vale, R D.]]
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[[Category: Vale RD]]
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[[Category: aaa atpase]]
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[[Category: atp-binding]]
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[[Category: hydrolase]]
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[[Category: nucleotide-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:24:26 2008''
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Current revision

Spastin

PDB ID 3b9p

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