1h7c

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[[Image:1h7c.gif|left|200px]]
 
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{{Structure
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==human tubulin chaperone cofactor a==
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|PDB= 1h7c |SIZE=350|CAPTION= <scene name='initialview01'>1h7c</scene>, resolution 1.8&Aring;
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<StructureSection load='1h7c' size='340' side='right'caption='[[1h7c]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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<table><tr><td colspan='2'>[[1h7c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H7C 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]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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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=1h7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7c OCA], [https://pdbe.org/1h7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h7c RCSB], [https://www.ebi.ac.uk/pdbsum/1h7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h7c ProSAT]</span></td></tr>
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</table>
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'''HUMAN TUBULIN CHAPERONE COFACTOR A'''
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== Function ==
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[https://www.uniprot.org/uniprot/TBCA_HUMAN TBCA_HUMAN] Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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alpha and beta-Tubulin fold in a series of chaperone-assisted steps. At least five protein cofactors are involved in the post-chaperonin tubulin folding pathway and required to maintain the supply of tubulin; some of them also participate in microtubule dynamics. The first tubulin chaperone identified in the tubulin folding pathway was cofactor A (CoA). Here we describe the three-dimensional structure of human CoA at 1.7 A resolution, determined by multiwavelength anomalous diffraction (MAD). The structure is a monomer with a rod-like shape and consists of a three-alpha-helix bundle, or coiled coil, with the second helix kinked by a proline break, offering a convex surface at one face of the protein. The helices are connected by short turns, one of them, between alpha2 and alpha3, including a 3(10)-helix. Peptide mapping analysis and competition experiments with peptides show that CoA interacts with beta-tubulin via the three alpha-helical regions but not with the rod-end loops. The main interaction occurs with the middle kinked alpha2 helix, at the convex face of the rod. Strong 3D structural homology is found with the Hsp70 chaperone cofactor BAG domain, suggesting that these proteins define a family of cofactors of simple compact architecture. Further structural homology is found with alpha-spectrin/alpha-actinin repeats, all are rods of identical length of ten helical turns. We propose to call these three-helix bundles alpha ten modules.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h7/1h7c_consurf.spt"</scriptWhenChecked>
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1H7C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7C OCA].
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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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==Reference==
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</jmolCheckbox>
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Three-dimensional structure of human tubulin chaperone cofactor A., Guasch A, Aloria K, Perez R, Avila J, Zabala JC, Coll M, J Mol Biol. 2002 May 10;318(4):1139-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12054808 12054808]
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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=1h7c ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aloria, K.]]
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[[Category: Aloria K]]
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[[Category: Avila, J.]]
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[[Category: Avila J]]
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[[Category: Campo, R.]]
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[[Category: Campo R]]
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[[Category: Coll, M.]]
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[[Category: Coll M]]
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[[Category: Guasch, A.]]
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[[Category: Guasch A]]
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[[Category: Perez, R.]]
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[[Category: Perez R]]
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[[Category: Zabala, J C.]]
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[[Category: Zabala JC]]
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[[Category: ACY]]
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[[Category: SO4]]
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[[Category: chaperone]]
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[[Category: cofactor some]]
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[[Category: p14]]
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[[Category: protein folding]]
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[[Category: tubulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:33:14 2008''
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Current revision

human tubulin chaperone cofactor a

PDB ID 1h7c

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