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1fw2

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Revision as of 06:13, 3 January 2018

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI

Structural highlights

1fw2 is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1qd5, 1qd6
Activity:	Phospholipase A(1), with EC number 3.1.1.32
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PA1_ECOLI] Has broad substrate specificity including hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to outer membrane breakdown and cell death; is dormant in normal growing cells. Required for efficient secretion of bacteriocins.

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 PubMed

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.

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

↑ Snijder HJ, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW. Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli. J Mol Biol. 2001 Jun 1;309(2):477-89. PMID:11371166 doi:10.1006/jmbi.2001.4675

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fw2"

@@ Line 1: / Line 1: @@
 ==OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI==
 <StructureSection load='1fw2' size='340' side='right' caption='[[1fw2]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qd5|1qd5]], [[1qd6|1qd6]]</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 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=1fw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fw2 OCA], [http://pdbe.org/1fw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1fw2 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=1fw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fw2 OCA], [http://pdbe.org/1fw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1fw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fw2 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/1fw2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/1fw2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1fw2

From Proteopedia

Revision as of 06:13, 3 January 2018

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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