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New page: left|200px<br /><applet load="1dk5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dk5, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1dk5.jpg|left|200px]]<br /><applet load="1dk5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dk5, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF ANNEXIN 24(CA32) FROM CAPSICUM ANNUUM'''<br />


==Overview==
==CRYSTAL STRUCTURE OF ANNEXIN 24(CA32) FROM CAPSICUM ANNUUM==
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.
<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 [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='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='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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dk/1dk5_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=1dk5 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1DK5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Capsicum_annuum Capsicum annuum] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DK5 OCA].
*[[Annexin 3D structures|Annexin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10713128 10713128]
[[Category: Capsicum annuum]]
[[Category: Capsicum annuum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dorowski, A.]]
[[Category: Dorowski A]]
[[Category: Hofmann, A.]]
[[Category: Hofmann A]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Proust, J.]]
[[Category: Proust J]]
[[Category: Schantz, R.]]
[[Category: Schantz R]]
[[Category: SO4]]
[[Category: bell pepper]]
[[Category: calcium binding protein]]
[[Category: capsicum annuum]]
[[Category: plant annexin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:13:50 2007''

Latest revision as of 06:54, 7 February 2024

CRYSTAL STRUCTURE OF ANNEXIN 24(CA32) FROM CAPSICUM ANNUUM

1dk5, resolution 2.80Å

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