1qd6: Difference between revisions

[[Image:1qd6.jpg|left|200px]]<br /><applet load="1qd6" size="350" color="white" frame="true" align="right" spinBox="true"  

Dimerization is a biological regulatory mechanism employed by both soluble and membrane proteins. However, there are few structural data on the factors that govern dimerization of membrane proteins. Outer membrane phospholipase A (OMPLA) is an integral membrane enzyme which participates in secretion of colicins in Escherichia coli. In Campilobacter and Helicobacter pylori strains, OMPLA is implied in virulence. Its activity is regulated by reversible dimerization. Here we report X-ray structures of monomeric and dimeric OMPLA from E. coli. Dimer interactions occur almost exclusively in the apolar membrane-embedded parts, with two hydrogen bonds within the hydrophobic membrane area being key interactions. Dimerization results in functional oxyanion holes and substrate-binding pockets, which are absent in monomeric OMPLA. These results provide a detailed view of activation by dimerization of a membrane protein.

1QD6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=HDS:'>HDS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(1) Phospholipase A(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.32 3.1.1.32] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QD6 OCA].  

[[Category: Dijkstra, B W.]]

[[Category: Egmond, M R.]]

[[Category: Kalk, K H.]]

[[Category: Snijder, H J.]]

[[Category: Verheij, H M.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:25 2008''