1dk5: Difference between revisions

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 ==CRYSTAL STRUCTURE OF ANNEXIN 24(CA32) FROM CAPSICUM ANNUUM==
-<StructureSection load='1dk5' size='340' side='right' caption='[[1dk5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='1dk5' size='340' side='right'caption='[[1dk5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dk5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bell_pepper Bell pepper]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DK5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DK5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dk5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Capsicum_annuum Capsicum annuum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DK5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=1dk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk5 OCA], [http://pdbe.org/1dk5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dk5 RCSB], [http://www.ebi.ac.uk/pdbsum/1dk5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dk5 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1dk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk5 OCA], [https://pdbe.org/1dk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dk5 RCSB], [https://www.ebi.ac.uk/pdbsum/1dk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dk5 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q42657_CAPAN Q42657_CAPAN]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 20: @@
 </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=1dk5 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-This work provides the first three-dimensional structure of a member of the plant annexin family and correlates these findings with biochemical properties of this protein. Annexin 24(Ca32) from Capsicum annuum was purified as a native protein from bell pepper and was also prepared by recombinant techniques. To overcome the problem of precipitation of the recombinant wild-type protein in crystallization trials, two mutants were designed. Whereas an N-terminal truncation mutant turned out to be an unstable protein, the N-terminal His-tagged annexin 24(Ca32) was crystallized, and the three-dimensional structure was determined by x-ray diffraction at 2. 8 A resolution. The structure refined to an R-factor of 0.216 adopts the typical annexin fold; the detailed structure, however, is different from non-plant annexins, especially in domains I and III and in the membrane binding loops on the convex side. Within the unit cell there are two molecules per asymmetric unit, which differ in conformation of the IAB-loop. Both conformers show Trp-35 on the surface. The loop-out conformation is stabilized by tight interactions of this tryptophan with residue side chains of a symmetry-related molecule and enforced by a bound sulfate. Characterization of this plant annexin using biophysical methods revealed calcium-dependent binding to phospholipid vesicles with preference for phosphatidylcholine over phosphatidylserine and magnesium-dependent phosphodiesterase activity in vitro as shown with adenosine triphosphate as the substrate. A comparative unfolding study of recombinant annexin 24(Ca32) wild type and of the His-tag fusion protein indicates higher stability of the latter. The effect of this N-terminal modification is also visible from CD spectra. Both proteins were subjected to a FURA-2-based calcium influx assay, which gave high influx rates for the wild-type but greatly reduced influx rates for the fusion protein. We therefore conclude that the N-terminal domain is indeed a major regulatory element modulating different annexin properties by allosteric mechanisms.
-Annexin 24 from Capsicum annuum. X-ray structure and biochemical characterization.,Hofmann A, Proust J, Dorowski A, Schantz R, Huber R J Biol Chem. 2000 Mar 17;275(11):8072-82. PMID:10713128<ref>PMID:10713128</ref>
+==See Also==
+*[[Annexin 3D structures|Annexin 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1dk5" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bell pepper]]
-[[Category: Dorowski, A]]
-[[Category: Hofmann, A]]
-[[Category: Huber, R]]
-[[Category: Proust, J]]
-[[Category: Schantz, R]]
-[[Category: Calcium binding protein]]
 [[Category: Capsicum annuum]]
-[[Category: Metal binding protein]]
+[[Category: Large Structures]]
-[[Category: Plant annexin]]
+[[Category: Dorowski A]]
+[[Category: Hofmann A]]
+[[Category: Huber R]]
+[[Category: Proust J]]
+[[Category: Schantz R]]