1fw3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fw3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FW3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1fw3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FW3 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=S1H:1-HEXADECANOSULFONYL-O-L-SERINE'>S1H</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=S1H:1-HEXADECANOSULFONYL-O-L-SERINE'>S1H</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qd5|1qd5]], [[1qd6|1qd6]], [[1fw2|1fw2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qd5|1qd5]], [[1qd6|1qd6]], [[1fw2|1fw2]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fw3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fw3 RCSB], [http://www.ebi.ac.uk/pdbsum/1fw3 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fw3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fw3 RCSB], [http://www.ebi.ac.uk/pdbsum/1fw3 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Dekker, N | [[Category: Dekker, N]] | ||
[[Category: Dijkstra, B W | [[Category: Dijkstra, B W]] | ||
[[Category: Egmond, M R | [[Category: Egmond, M R]] | ||
[[Category: Kalk, K H | [[Category: Kalk, K H]] | ||
[[Category: Kingma, R L | [[Category: Kingma, R L]] | ||
[[Category: Snijder, H J | [[Category: Snijder, H J]] | ||
[[Category: Anti-parallel beta barrel dimer]] | [[Category: Anti-parallel beta barrel dimer]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
Revision as of 02:38, 23 December 2014
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLIOUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedOuter 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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