1pp2: Difference between revisions

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[[Image:1pp2.gif|left|200px]]<br /><applet load="1pp2" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1pp2.gif|left|200px]]
caption="1pp2, resolution 2.5&Aring;" />
 
'''THE REFINED CRYSTAL STRUCTURE OF DIMERIC PHOSPHOLIPASE A2 AT 2.5 ANGSTROMS. ACCESS TO A SHIELDED CATALYTIC CENTER'''<br />
{{Structure
|PDB= 1pp2 |SIZE=350|CAPTION= <scene name='initialview01'>1pp2</scene>, resolution 2.5&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [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]
|GENE=
}}
 
'''THE REFINED CRYSTAL STRUCTURE OF DIMERIC PHOSPHOLIPASE A2 AT 2.5 ANGSTROMS. ACCESS TO A SHIELDED CATALYTIC CENTER'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1PP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1PP2 OCA].  
1PP2 is a [[Single protein]] structure of sequence 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==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=4019493 4019493]
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:[http://www.ncbi.nlm.nih.gov/pubmed/4019493 4019493]
[[Category: Crotalus atrox]]
[[Category: Crotalus atrox]]
[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
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[[Category: hydrolase]]
[[Category: hydrolase]]


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Revision as of 14:27, 20 March 2008

File:1pp2.gif


PDB ID 1pp2

Drag the structure with the mouse to rotate
, resolution 2.5Å
Activity: Phospholipase A(2), with EC number 3.1.1.4
Coordinates: save as pdb, mmCIF, xml



THE REFINED CRYSTAL STRUCTURE OF DIMERIC PHOSPHOLIPASE A2 AT 2.5 ANGSTROMS. ACCESS TO A SHIELDED CATALYTIC CENTER


OverviewOverview

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.

About this StructureAbout this Structure

1PP2 is a Single protein structure of sequence from Crotalus atrox. Full crystallographic information is available from OCA.

ReferenceReference

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

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