1hn4

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(New page: 200px<br /><applet load="1hn4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hn4, resolution 1.5&Aring;" /> '''PROPHOSPHOLIPASE A2 D...)
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[[Image:1hn4.jpg|left|200px]]<br /><applet load="1hn4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hn4, resolution 1.5&Aring;" />
 
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'''PROPHOSPHOLIPASE A2 DIMER COMPLEXED WITH MJ33, SULFATE, AND CALCIUM'''<br />
 
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==Overview==
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==PROPHOSPHOLIPASE A2 DIMER COMPLEXED WITH MJ33, SULFATE, AND CALCIUM==
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Kinetic results in this paper show that, contrary to earlier reports, pig, pancreatic prophospholipase A(2) (proPLA2) does not hydrolyze monodisperse, short chain phosphatidylcholine below the critical micelle concentration., ProPLA2 is active on an anionic interface, but at a rate that is decreased, by more than 100-fold compared to that of PLA2, the active form. Solution, studies show that both proPLA2 and PLA2 bind to an anionic interface and, also bind a tetrahedral intermediate mimic at the active site. The 1.5 A, resolution crystal structure of the anion-assisted dimer of proPLA2, reported in this paper is compared with the corresponding structure for, PLA2 [Pan, Y. H., et al. (2001) Biochemistry 40, 609-617]. As a mimic for, the forms bound to the anionic interface, these structures provide, insights into the possible structural basis for the impaired chemical step, of the zymogen. The proPLA2 dimer contained within one crystallographic, asymmetric unit has one molecule of the inhibitor, 1-hexadecyl-3-(trifluoroethyl)-sn-glycero-2-phosphomethanol and is bridged, by four coplanar sulfate anions. Relative to the structure of PLA2, the, subunit contact surface in proPLA2 displays a tilted orientation, an, altered mode of inhibitor binding, displacement of a mechanistically, significant loop that includes Tyr69, and a critical active site water, seen in PLA2 that is not seen in proPLA2. These differences are, interpreted to suggest possible origins of the functional differences, between the pro and active enzyme at an anionic interface. A structural, origin of this difference is discussed in terms of the calcium-coordinated, activated water mechanism of the esterolysis reaction. Together, a, comparison of the structures of the anion-assisted dimers of PLA2 and, proPLA2 not only offers an explanation of why the zymogen form is, k(cat)-impaired and binds poorly even to the anionic interface but also, supports a mechanism for the activated enzyme that includes a critical, second-sphere assisting water bridging His48 and the calcium-coordinated, catalytic water.
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<StructureSection load='1hn4' size='340' side='right'caption='[[1hn4]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hn4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HN4 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]] 1.5&#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>, <scene name='pdbligand=MJI:1-HEXADECYL-3-TRIFLUOROETHYL-SN-GLYCERO-2-PHOSPHATE+METHANE'>MJI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1hn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn4 OCA], [https://pdbe.org/1hn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hn4 RCSB], [https://www.ebi.ac.uk/pdbsum/1hn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hn4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PA21B_PIG PA21B_PIG] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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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/hn/1hn4_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=1hn4 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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1HN4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA, SO4 and MJI as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HN4 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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The basis for k(cat) impairment in prophospholipase A(2) from the anion-assisted dimer structure., Epstein TM, Yu BZ, Pan YH, Tutton SP, Maliwal BP, Jain MK, Bahnson BJ, Biochemistry. 2001 Sep 25;40(38):11411-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11560489 11560489]
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[[Category: Large Structures]]
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[[Category: Phospholipase A(2)]]
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[[Category: Single protein]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Bahnson, B.J.]]
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[[Category: Bahnson BJ]]
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[[Category: Epstein, T.M.]]
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[[Category: Epstein TM]]
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[[Category: Jain, M.K.]]
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[[Category: Jain MK]]
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[[Category: Pan, Y.H.]]
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[[Category: Pan YH]]
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[[Category: CA]]
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[[Category: MJI]]
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[[Category: SO4]]
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[[Category: carboxylic ester hydrolase]]
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[[Category: dimer]]
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[[Category: enzyme]]
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[[Category: hydrolase]]
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[[Category: inhibitor binding]]
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[[Category: sulfate binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:40:05 2007''
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Current revision

PROPHOSPHOLIPASE A2 DIMER COMPLEXED WITH MJ33, SULFATE, AND CALCIUM

PDB ID 1hn4

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