1wab: Difference between revisions

No edit summary
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1wab.gif|left|200px]]<br /><applet load="1wab" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1wab, resolution 1.7&Aring;" />
'''PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE'''<br />


==Overview==
==PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE==
The platelet-activating factor PAF (1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine) is a potent lipid first messenger active in general cell activation, fertilization, inflammatory and allergic reactions, asthma, HIV pathogenesis, carcinogenesis, and apoptosis. There is substantial evidence that PAF is involved in intracellular signalling, but the pathways are poorly understood. Inactivation of PAF is carried out by specific intra- and extracellular acetylhydrolases (PAF-AHs), a subfamily of phospholipases A2 that remove the sn-2 acetyl group. Mammalian brain contains at least three intracellular isoforms, of which PAF-AH(Ib) is the best characterized. This isoform contains a heterodimer of two homologous catalytic subunits alpha1 and alpha2, each of relative molecular mass 26K, and a non-catalytic 45K beta-subunit, a homologue of the beta-subunit of trimeric G proteins. We now report the crystal structure of the bovine alpha1 subunit of PAF-AH(Ib) at 1.7 A resolution in complex with a reaction product, acetate. The tertiary fold of this protein is closely reminiscent of that found in p21(ras) and other GTPases. The active site is made up of a trypsin-like triad of Ser 47, His 195 and Asp 192. Thus, the intact PAF-AH(Ib) molecule is an unusual G-protein-like (alpha1/alpha2)beta trimer.
<StructureSection load='1wab' size='340' side='right'caption='[[1wab]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wab]] is a 1 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=1WAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WAB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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=1wab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wab OCA], [https://pdbe.org/1wab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wab RCSB], [https://www.ebi.ac.uk/pdbsum/1wab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wab ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wa/1wab_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1wab ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1WAB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=ACT:'>ACT</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAB OCA].
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer., Ho YS, Swenson L, Derewenda U, Serre L, Wei Y, Dauter Z, Hattori M, Adachi T, Aoki J, Arai H, Inoue K, Derewenda ZS, Nature. 1997 Jan 2;385(6611):89-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8985254 8985254]
[[Category: 1-alkyl-2-acetylglycerophosphocholine esterase]]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Adachi, T.]]
[[Category: Adachi T]]
[[Category: Aoki, J.]]
[[Category: Aoki J]]
[[Category: Arai, H.]]
[[Category: Arai H]]
[[Category: Dauter, Z.]]
[[Category: Dauter Z]]
[[Category: Derewenda, U.]]
[[Category: Derewenda U]]
[[Category: Derewenda, Z S.]]
[[Category: Derewenda ZS]]
[[Category: Hattori, M.]]
[[Category: Hattori M]]
[[Category: Ho, Y S.]]
[[Category: Ho YS]]
[[Category: Inoue, K.]]
[[Category: Inoue K]]
[[Category: Serre, L.]]
[[Category: Serre L]]
[[Category: Swenson, L.]]
[[Category: Swenson L]]
[[Category: Wei, Y.]]
[[Category: Wei Y]]
[[Category: ACT]]
[[Category: fad]]
[[Category: flavoprotein]]
[[Category: oxidoreductase]]
[[Category: peroxisome]]
[[Category: platelet factor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:09 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA