1fw3: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1fw3.png|left|200px]]
-<!--
+==OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI==
-The line below this paragraph, containing "STRUCTURE_1fw3", creates the "Structure Box" on the page.
+<StructureSection load='1fw3' size='340' side='right'caption='[[1fw3]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1fw3]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1FW3 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=S1H:1-HEXADECANOSULFONYL-O-L-SERINE'>S1H</scene></td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fw3 OCA], [https://pdbe.org/1fw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fw3 RCSB], [https://www.ebi.ac.uk/pdbsum/1fw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fw3 ProSAT]</span></td></tr>
-{{STRUCTURE_1fw3|  PDB=1fw3  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PA1_ECOLI 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/1fw3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fw3 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI===
+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<ref>PMID:11371166</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11371166}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1fw3" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11371166 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11371166}}
+__TOC__
+</StructureSection>
-==About this Structure==
-FW3 is a 2 chains structure of sequences 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].
-==Reference==
-<ref group="xtra">PMID:11371166</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Dekker, N.]]
+[[Category: Large Structures]]
-[[Category: Dijkstra, B W.]]
+[[Category: Dekker N]]
-[[Category: Egmond, M R.]]
+[[Category: Dijkstra BW]]
-[[Category: Kalk, K H.]]
+[[Category: Egmond MR]]
-[[Category: Kingma, R L.]]
+[[Category: Kalk KH]]
-[[Category: Snijder, H J.]]
+[[Category: Kingma RL]]
-[[Category: Anti-parallel beta barrel dimer]]
+[[Category: Snijder HJ]]
-[[Category: Membrane protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 01:51:07 2009''