1dk5

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[[Image:1dk5.jpg|left|200px]]<br /><applet load="1dk5" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dk5.jpg|left|200px]]
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caption="1dk5, resolution 2.8&Aring;" />
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'''CRYSTAL STRUCTURE OF ANNEXIN 24(CA32) FROM CAPSICUM ANNUUM'''<br />
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{{Structure
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|PDB= 1dk5 |SIZE=350|CAPTION= <scene name='initialview01'>1dk5</scene>, resolution 2.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF ANNEXIN 24(CA32) FROM CAPSICUM ANNUUM'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DK5 OCA].
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1DK5 is a [[Single protein]] structure of sequence from [http://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].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/10713128 10713128]
[[Category: Capsicum annuum]]
[[Category: Capsicum annuum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: plant annexin]]
[[Category: plant annexin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:39:52 2008''

Revision as of 08:39, 20 March 2008


PDB ID 1dk5

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF ANNEXIN 24(CA32) FROM CAPSICUM ANNUUM


Overview

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.

About this Structure

1DK5 is a Single protein structure of sequence from Capsicum annuum. Full crystallographic information is available from OCA.

Reference

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

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