1p2p: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1p2p.gif|left|200px]]
{{Seed}}
[[Image:1p2p.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p2p|  PDB=1p2p  |  SCENE=  }}  
{{STRUCTURE_1p2p|  PDB=1p2p  |  SCENE=  }}  


'''STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2 AT 2.6 ANGSTROMS RESOLUTION AND COMPARISON WITH BOVINE PHOSPHOLIPASE A2'''
===STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2 AT 2.6 ANGSTROMS RESOLUTION AND COMPARISON WITH BOVINE PHOSPHOLIPASE A2===




==Overview==
<!--  
The previously published three-dimensional structure of porcine pancreatic prophospholipase A2 at 3 A resolution was found to be incompatible with the structures of bovine phospholipase A2 and bovine prophospholipase A2. This was unexpected because of the very homologous amino acid sequences of these enzymes. Therefore, the crystal structure of the porcine enzyme was redetermined using molecular replacement methods with bovine phospholipase as the parent model. The structure was crystallographically refined at 2.6 A resolution by fast Fourier transform and restrained least-squares procedures to an R-factor of 0.241. The crystals appeared to contain phospholipase A2 and not prophospholipase A2. Apparently the protein is slowly converted under the crystallization conditions employed. Our investigation shows that, in contrast to the previous report, the three-dimensional structure of porcine phospholipase A2 is very similar to that of bovine phospholipase A2, including the active site. Smaller differences were observed in some residues involved in the binding of aggregated substrates. However, an appreciable conformational difference is in the loop 59 to 70, where a single substitution at position 63 (bovine Val leads to porcine Phe) causes a complete rearrangement of the peptide chain. In addition to the calcium ion in the active site, a second calcium ion is present in the crystals; this is located on a crystallographic 2-fold axis and stabilizes the interaction between two neighbouring molecules.
The line below this paragraph, {{ABSTRACT_PUBMED_6876174}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 6876174 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_6876174}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Renetseder, R.]]
[[Category: Renetseder, R.]]
[[Category: Carboxylic ester hydrolase]]
[[Category: Carboxylic ester hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:36:21 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:19:35 2008''

Revision as of 23:19, 28 July 2008

File:1p2p.png

Template:STRUCTURE 1p2p

STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2 AT 2.6 ANGSTROMS RESOLUTION AND COMPARISON WITH BOVINE PHOSPHOLIPASE A2

Template:ABSTRACT PUBMED 6876174

About this Structure

1P2P is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Structure of porcine pancreatic phospholipase A2 at 2.6 A resolution and comparison with bovine phospholipase A2., Dijkstra BW, Renetseder R, Kalk KH, Hol WG, Drenth J, J Mol Biol. 1983 Jul 25;168(1):163-79. PMID:6876174

Page seeded by OCA on Tue Jul 29 02:19:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1p2p&oldid=722823"