1jia

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[[Image:1jia.gif|left|200px]]<br />
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[[Image:1jia.gif|left|200px]]<br /><applet load="1jia" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1jia" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1jia, resolution 2.13&Aring;" />
caption="1jia, resolution 2.13&Aring;" />
'''STRUCTURE OF A BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS AT 2.13A RESOLUTION'''<br />
'''STRUCTURE OF A BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS AT 2.13A RESOLUTION'''<br />
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==About this Structure==
==About this Structure==
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1JIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gloydius_halys Gloydius halys] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Structure known Active Sites: ATA and ATB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JIA OCA].
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1JIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gloydius_halys Gloydius halys] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Sites: <scene name='pdbsite=ATA:Active Site'>ATA</scene> and <scene name='pdbsite=ATB:Active Site'>ATB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JIA OCA].
==Reference==
==Reference==
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[[Category: phospholipase a2]]
[[Category: phospholipase a2]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:40:36 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:36:32 2007''

Revision as of 14:26, 18 December 2007


1jia, resolution 2.13Å

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STRUCTURE OF A BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS AT 2.13A RESOLUTION

Overview

The basic phospholipase A2 isolated from the venom of Agkistrodon halys, Pallas (Agkistrodon blomhoffii Brevicaudus) is a hemolytic toxin and one, of the few PLA2's capable of hydrolyzing the phospholipids of E. coli, membranes in the presence of a bactericidal/permeability-increasing, protein (BPI) of neutrophils. The crystal structure has been determined, and refined at 2.13 A to an R factor of 16.5% (F > 3sigma) with excellent, stereochemistry. A superposition of the two molecules in the asymmetric, unit gives an r. m.s. deviation of 0.326 A for all Calpha atoms. The, refined structure allowed a detailed comparison with other PLA2 species of, known structures. The overall architecture is similar to those of other, PLA2's with a few significant differences. One of which is in the region, connecting the N-terminal helix and the Ca2+-binding loop. Unexpectedly, the conformation of the peptide plane Cys29-Gly30 in the Ca2+-binding loop, is very different to that of other PLA2's. The amide NH of Gly30 does not, point toward the proposed site for stabilization of the tetrahedral, intermediate oxyanion of the substrate analogue. The structure includes, four residues which occur less frequently in other PLA2's. His1, Arg6 and, Trp70 located at the interfacial recognition site may play an important, role in the interaction with aggregated substrates, while Trp77, contributes to the hydrophobic interactions between the beta-wing and the, main body of the molecule. This structure analysis reveals that two, clusters of basic residues are located at or near the interfacial, recognition site, forming an asymmetric positively charge distribution. In, contrast to the acidic isoform, the present enzyme is a dimer in the, crystalline state. The special phospholipid hydrolysis behaviors are, discussed in the light of the structure determined.

About this Structure

1JIA is a Single protein structure of sequence from Gloydius halys with CA as ligand. Active as Phospholipase A(2), with EC number 3.1.1.4 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

Structure of a basic phospholipase A2 from Agkistrodon halys Pallas at 2.13 A resolution., Zhao K, Song S, Lin Z, Zhou Y, Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):510-21. PMID:9761847

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