1fw3
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1fw3.jpg|left|200px]] | [[Image:1fw3.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1fw3", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1fw3| PDB=1fw3 | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI''' | '''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI''' | ||
| Line 24: | Line 21: | ||
Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli., Snijder HJ, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW, J Mol Biol. 2001 Jun 1;309(2):477-89. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11371166 11371166] | Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli., Snijder HJ, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW, J Mol Biol. 2001 Jun 1;309(2):477-89. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11371166 11371166] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Phospholipase A(1)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dekker, N.]] | [[Category: Dekker, N.]] | ||
| Line 32: | Line 28: | ||
[[Category: Kingma, R L.]] | [[Category: Kingma, R L.]] | ||
[[Category: Snijder, H J.]] | [[Category: Snijder, H J.]] | ||
| - | [[Category: | + | [[Category: Anti-parallel beta barrel dimer]] |
| - | [[Category: | + | [[Category: Membrane protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:49:53 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:49, 2 May 2008
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI
Overview
Outer membrane phospholipase A (OMPLA) is an integral membrane enzyme that catalyses the hydrolysis of phospholipids. Enzymatic activity is regulated by reversible dimerisation and calcium-binding. We have investigated the role of calcium by X-ray crystallography. In monomeric OMPLA, one calcium ion binds between two external loops (L3L4 site) at 10 A from the active site. After dimerisation, a new calcium-binding site (catalytic site) is formed at the dimer interface in the active site of each molecule at 6 A from the L3L4 calcium site. The close spacing and the difference in calcium affinity of both sites suggests that the L3L4 site may function as a storage site for a calcium ion, which relocates to the catalytic site upon dimerisation. A sequence alignment demonstrates conservation of the catalytic calcium site but evolutionary variation of the L3L4 site. The residues in the dimer interface are conserved as well, suggesting that all outer membrane phospholipases require dimerisation and calcium in the catalytic site for activity. For this family of phospholipases, we have characterised a consensus sequence motif (YTQ-X(n)-G-X(2)-H-X-SNG) that contains conserved residues involved in dimerisation and catalysis.
About this Structure
1FW3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli., Snijder HJ, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW, J Mol Biol. 2001 Jun 1;309(2):477-89. PMID:11371166 Page seeded by OCA on Fri May 2 16:49:53 2008
