1pob

From Proteopedia

(Difference between revisions)

Current revision

CRYSTAL STRUCTURE OF COBRA-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE

Structural highlights

1pob is a 2 chain structure with sequence from Naja atra. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PA2A1_NAJAT Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.^[1] ^[2]

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

The crystal structure of a complex between a phosphonate transition-state analogue and the phospholipase A2 (PLA2) from Naja naja atra venom has been solved and refined to a resolution of 2.0 angstroms. The identical stereochemistry of the two complexes that comprise the crystal's asymmetric unit indicates both the manner in which the transition state is stabilized and how the hydrophobic fatty acyl chains of the substrate are accommodated by the enzyme during interfacial catalysis. The critical features that suggest the chemistry of binding and catalysis are the same as those seen in the crystal structure of a similar complex formed with the evolutionarily distant bee-venom PLA2.

Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue.,White SP, Scott DL, Otwinowski Z, Gelb MH, Sigler PB Science. 1990 Dec 14;250(4987):1560-3. PMID:2274787^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Huang LF, Zheng JB, Xu Y, Song HT, Yu CX. A snake venom phospholipase A2 with high affinity for muscarinic acetylcholine receptors acts on guinea pig ileum. Toxicon. 2008 May;51(6):1008-16. doi: 10.1016/j.toxicon.2008.01.006. Epub 2008, Jan 17. PMID:18281071 doi:http://dx.doi.org/10.1016/j.toxicon.2008.01.006
↑ Kini RM, Evans HJ. Structure-function relationships of phospholipases. The anticoagulant region of phospholipases A2. J Biol Chem. 1987 Oct 25;262(30):14402-7. PMID:3117784
↑ White SP, Scott DL, Otwinowski Z, Gelb MH, Sigler PB. Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue. Science. 1990 Dec 14;250(4987):1560-3. PMID:2274787

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-[[Image:1pob.gif|left|200px]]<br /><applet load="1pob" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1pob, resolution 2.0&Aring;" />
-'''CRYSTAL STRUCTURE OF COBRA-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF COBRA-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE==
-The crystal structure of a complex between a phosphonate transition-state, analogue and the phospholipase A2 (PLA2) from Naja naja atra venom has, been solved and refined to a resolution of 2.0 angstroms. The identical, stereochemistry of the two complexes that comprise the crystal's, asymmetric unit indicates both the manner in which the transition state is, stabilized and how the hydrophobic fatty acyl chains of the substrate are, accommodated by the enzyme during interfacial catalysis. The critical, features that suggest the chemistry of binding and catalysis are the same, as those seen in the crystal structure of a similar complex formed with, the evolutionarily distant bee-venom PLA2.
+<StructureSection load='1pob' size='340' side='right'caption='[[1pob]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1pob]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1POB FirstGlance]. <br>
+</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&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GEL:1-O-OCTYL-2-HEPTYLPHOSPHONYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>GEL</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=1pob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pob OCA], [https://pdbe.org/1pob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pob RCSB], [https://www.ebi.ac.uk/pdbsum/1pob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pob ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PA2A1_NAJAT PA2A1_NAJAT] Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:18281071</ref> <ref>PMID:3117784</ref>
+== 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/po/1pob_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=1pob ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of a complex between a phosphonate transition-state analogue and the phospholipase A2 (PLA2) from Naja naja atra venom has been solved and refined to a resolution of 2.0 angstroms. The identical stereochemistry of the two complexes that comprise the crystal's asymmetric unit indicates both the manner in which the transition state is stabilized and how the hydrophobic fatty acyl chains of the substrate are accommodated by the enzyme during interfacial catalysis. The critical features that suggest the chemistry of binding and catalysis are the same as those seen in the crystal structure of a similar complex formed with the evolutionarily distant bee-venom PLA2.
-==About this Structure==
+Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue.,White SP, Scott DL, Otwinowski Z, Gelb MH, Sigler PB Science. 1990 Dec 14;250(4987):1560-3. PMID:2274787<ref>PMID:2274787</ref>
-POB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra] with CA and GEL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1POB OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue., White SP, Scott DL, Otwinowski Z, Gelb MH, Sigler PB, Science. 1990 Dec 14;250(4987):1560-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2274787 2274787]
+</div>
-[[Category: Naja atra]]
+<div class="pdbe-citations 1pob" style="background-color:#fffaf0;"></div>
-[[Category: Phospholipase A(2)]]
-[[Category: Single protein]]
-[[Category: Otwinowski, Z.]]
-[[Category: Scott, D.L.]]
-[[Category: Sigler, P.B.]]
-[[Category: White, S.P.]]
-[[Category: CA]]
-[[Category: GEL]]
-[[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:58:10 2007''
+==See Also==
+*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Naja atra]]
+[[Category: Otwinowski Z]]
+[[Category: Scott DL]]
+[[Category: Sigler PB]]
+[[Category: White SP]]

1pob

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF COBRA-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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