1pp2: Difference between revisions

No edit summary
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:1pp2.png|left|200px]]


<!--
==THE REFINED CRYSTAL STRUCTURE OF DIMERIC PHOSPHOLIPASE A2 AT 2.5 ANGSTROMS. ACCESS TO A SHIELDED CATALYTIC CENTER==
The line below this paragraph, containing "STRUCTURE_1pp2", creates the "Structure Box" on the page.
<StructureSection load='1pp2' size='340' side='right'caption='[[1pp2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1pp2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PP2 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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=1pp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pp2 OCA], [https://pdbe.org/1pp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pp2 RCSB], [https://www.ebi.ac.uk/pdbsum/1pp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pp2 ProSAT]</span></td></tr>
{{STRUCTURE_1pp2|  PDB=1pp2  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/PA2A_CROAT PA2A_CROAT] PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
== 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/pp/1pp2_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=1pp2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 2.5-A crystal structure of the calcium-free form of the dimeric venom phospholipase A2 from the Western Diamondback rattlesnake Crotalus atrox, has been refined to an R-factor of 17.8% (I greater than 2 sigma) and acceptable stereochemistry. The molecule is a nearly perfect 2-fold symmetric dimer in which most of the catalytic residues of both subunits face an internal cavity. The restricted access to the putative catalytic sites is especially puzzling as the optimal substrates for this and most other phospholipase A2 are phospholipids condensed in micellar or lamellar aggregates. We point out that substrate access to the internal cavity may be aided by calcium binding which can alter the intersubunit contacts that shield the catalytic network. We also suggest that a system of hydrogen-bonded moieties exists on the surface of the dimer that links the amino terminus to the catalytic system, through an invariant Gln 4 side chain and the backbone of the active center residue, Tyr 73. This hydrogen-bonded network is on a highly accessible surface of the dimer and would appear to contribute to the enzyme's (as opposed to the proenzyme's) special capacity to attack aggregated rather than monomeric substrate.


===THE REFINED CRYSTAL STRUCTURE OF DIMERIC PHOSPHOLIPASE A2 AT 2.5 ANGSTROMS. ACCESS TO A SHIELDED CATALYTIC CENTER===
The refined crystal structure of dimeric phospholipase A2 at 2.5 A. Access to a shielded catalytic center.,Brunie S, Bolin J, Gewirth D, Sigler PB J Biol Chem. 1985 Aug 15;260(17):9742-9. PMID:4019493<ref>PMID:4019493</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pp2" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_4019493}}, adds the Publication Abstract to the page
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 4019493 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_4019493}}
__TOC__
 
</StructureSection>
==About this Structure==
1PP2 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PP2 OCA].
 
==Reference==
<ref group="xtra">PMID:4019493</ref><references group="xtra"/>
[[Category: Crotalus atrox]]
[[Category: Crotalus atrox]]
[[Category: Brunie, S.]]
[[Category: Large Structures]]
[[Category: Sigler, P B.]]
[[Category: Brunie S]]
[[Category: Hydrolase]]
[[Category: Sigler PB]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:24:35 2009''

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

OCA