1o2e

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:22, 9 October 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1o2e.jpg|left|200px]]
 
-
<!--
+
==Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2==
-
The line below this paragraph, containing "STRUCTURE_1o2e", creates the "Structure Box" on the page.
+
<StructureSection load='1o2e' size='340' side='right'caption='[[1o2e]], [[Resolution|resolution]] 2.60&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'>[[1o2e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O2E FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANN:4-METHOXYBENZOIC+ACID'>ANN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-
{{STRUCTURE_1o2e| PDB=1o2e | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o2e OCA], [https://pdbe.org/1o2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o2e RCSB], [https://www.ebi.ac.uk/pdbsum/1o2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o2e ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PA21B_BOVIN PA21B_BOVIN] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
 +
== 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/o2/1o2e_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1o2e ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Phospholipase A2 catalyses the hydrolysis of the ester bond of 3-sn-phosphoglycerides. Here, we report the crystal structures of the free and anisic acid-bound triple mutant (K53,56,120M) of bovine pancreatic phospholipase A2. In the bound triple mutant structure, the small organic molecule p-anisic acid is found in the active site, and one of the carboxylate oxygen atoms is coordinated to the functionally important primary calcium ion. The other carboxylate oxygen atom is hydrogen bonded to the phenolic hydroxyl group of Tyr69. In addition, the bound anisic acid molecule replaces one of the functionally important water molecules in the active site. The residues 60-70, which are in a loop (surface loop), are disordered in most of the bovine pancreatic phospholipase A2 structures. It is interesting to note that these residues are ordered in the bound triple mutant structure but are disordered in the free triple mutant structure. The organic crystallization ingredient 2-methyl-2,4-pentanediol is found near the active site of the free triple mutant structure. The overall tertiary folding and stereochemical parameters for the final models of the free and anisic acid-bound triple mutant are virtually identical.
-
'''Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2'''
+
Crystal structures of the free and anisic acid bound triple mutant of phospholipase A2.,Sekar K, Vaijayanthi Mala S, Yogavel M, Velmurugan D, Poi MJ, Vishwanath BS, Gowda TV, Jeyaprakash AA, Tsai MD J Mol Biol. 2003 Oct 17;333(2):367-76. PMID:14529623<ref>PMID:14529623</ref>
-
 
+
-
 
+
-
==Overview==
+
-
Phospholipase A2 catalyses the hydrolysis of the ester bond of 3-sn-phosphoglycerides. Here, we report the crystal structures of the free and anisic acid-bound triple mutant (K53,56,120M) of bovine pancreatic phospholipase A2. In the bound triple mutant structure, the small organic molecule p-anisic acid is found in the active site, and one of the carboxylate oxygen atoms is coordinated to the functionally important primary calcium ion. The other carboxylate oxygen atom is hydrogen bonded to the phenolic hydroxyl group of Tyr69. In addition, the bound anisic acid molecule replaces one of the functionally important water molecules in the active site. The residues 60-70, which are in a loop (surface loop), are disordered in most of the bovine pancreatic phospholipase A2 structures. It is interesting to note that these residues are ordered in the bound triple mutant structure but are disordered in the free triple mutant structure. The organic crystallization ingredient 2-methyl-2,4-pentanediol is found near the active site of the free triple mutant structure. The overall tertiary folding and stereochemical parameters for the final models of the free and anisic acid-bound triple mutant are virtually identical.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
1O2E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O2E OCA].
+
</div>
 +
<div class="pdbe-citations 1o2e" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
Crystal structures of the free and anisic acid bound triple mutant of phospholipase A2., Sekar K, Vaijayanthi Mala S, Yogavel M, Velmurugan D, Poi MJ, Vishwanath BS, Gowda TV, Jeyaprakash AA, Tsai MD, J Mol Biol. 2003 Oct 17;333(2):367-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14529623 14529623]
+
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Sekar, K.]]
+
[[Category: Sekar K]]
-
[[Category: Tsai, M D.]]
+
[[Category: Tsai MD]]
-
[[Category: Velmurugan, D.]]
+
[[Category: Velmurugan D]]
-
[[Category: Alpha helix]]
+
-
[[Category: Anisic acid]]
+
-
[[Category: Beta sheet]]
+
-
[[Category: Triple mutant]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:16:07 2008''
+

Current revision

Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2

PDB ID 1o2e

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o2e"
Personal tools