1fxw

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(New page: 200px<br /><applet load="1fxw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fxw, resolution 2.1&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1fxw.gif|left|200px]]<br /><applet load="1fxw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fxw, resolution 2.1&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE RECOMBINANT ALPHA1/ALPHA2 CATALYTIC HETERODIMER OF BOVINE BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB.'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE RECOMBINANT ALPHA1/ALPHA2 CATALYTIC HETERODIMER OF BOVINE BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB.==
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The intracellular form of mammalian platelet activating factor, acetylhydrolase found in brain (PAF-AH Ib) is thought to play a critical, role in control in neuronal migration during cortex development. This, oligomeric complex consists of a homodimer of the 45 kDa (beta) LIS1, protein, the product of the causative gene for type I lissencephaly, and, depending on the developmental stage and species, one of three possible, pairs of two homologous approximately 26 kDa alpha-subunits, which harbor, all of the catalytic activity. The exact composition of this complex, depends on the expression patterns of the alpha(1) and alpha(2) genes, exhibiting tissue specificity and developmental control. All three, possible dimers (alpha(1)/alpha(1), alpha(1)/alpha(2) and, alpha(2)/alpha(2)) were identified in tissues. The alpha(1)/alpha(2), heterodimer is thought to play an important role in fetal brain. The, structure of the alpha(1)/alpha(1) homodimer was solved earlier in our, laboratory at 1.7 A. We report here the preparation of recombinant, alpha(1)/alpha(2) heterodimers using a specially constructed bi-cistronic, expression vector. The approach may be useful in studies of other systems, where pure heterodimers of recombinant proteins are required. The, alpha(1)/alpha(2) dimer has been crystallized and its structure was solved, at 2.1 A resolution by molecular replacement. These results set the stage, for a detailed characterization of the PAF-AH Ib complex.
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<StructureSection load='1fxw' size='340' side='right'caption='[[1fxw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fxw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FXW 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]] 2.1&#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=CA:CALCIUM+ION'>CA</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=1fxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fxw OCA], [https://pdbe.org/1fxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fxw RCSB], [https://www.ebi.ac.uk/pdbsum/1fxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fxw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PA1B3_BOVIN PA1B3_BOVIN] Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain.
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fx/1fxw_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1fxw ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FXW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/1-alkyl-2-acetylglycerophosphocholine_esterase 1-alkyl-2-acetylglycerophosphocholine esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.47 3.1.1.47] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FXW OCA].
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib., Sheffield PJ, McMullen TW, Li J, Ho YS, Garrard SM, Derewenda U, Derewenda ZS, Protein Eng. 2001 Jul;14(7):513-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11522926 11522926]
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[[Category: 1-alkyl-2-acetylglycerophosphocholine esterase]]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Derewenda, Z.]]
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[[Category: Derewenda Z]]
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[[Category: Li, J.]]
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[[Category: Li J]]
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[[Category: CA]]
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[[Category: alpha beta hydrolase fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:26:55 2007''
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Current revision

CRYSTAL STRUCTURE OF THE RECOMBINANT ALPHA1/ALPHA2 CATALYTIC HETERODIMER OF BOVINE BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB.

PDB ID 1fxw

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