3brx: Difference between revisions

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==Crystal Structure of calcium-bound cotton annexin Gh1==
==Crystal Structure of calcium-bound cotton annexin Gh1==
<StructureSection load='3brx' size='340' side='right' caption='[[3brx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3brx' size='340' side='right'caption='[[3brx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3brx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gossypium_hirsutum Gossypium hirsutum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BRX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BRX FirstGlance]. <br>
<table><tr><td colspan='2'>[[3brx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gossypium_hirsutum Gossypium hirsutum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BRX FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><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]] 2.5&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1n00|1n00]]</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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AnnGh1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3635 Gossypium hirsutum])</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=3brx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3brx OCA], [https://pdbe.org/3brx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3brx RCSB], [https://www.ebi.ac.uk/pdbsum/3brx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3brx ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3brx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3brx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3brx RCSB], [http://www.ebi.ac.uk/pdbsum/3brx PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[https://www.uniprot.org/uniprot/ANX1_GOSHI ANX1_GOSHI] Binds to phospholipid vesicles in a calcium-dependent manner in vitro (PubMed:16331990, PubMed:18441010). Prefers phosphatidyl-serine containing membranes. May have a role in the membrane cytoskeleton scaffolding or exocytotic processes (PubMed:16331990). May be involved in oxidative stress response (Probable).<ref>PMID:16331990</ref> <ref>PMID:18441010</ref> <ref>PMID:12787021</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/3brx_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/3brx_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=3brx ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plant annexins show distinct differences in comparison with their animal orthologues. In particular, the endonexin sequence, which is responsible for coordination of calcium ions in type II binding sites, is only partially conserved in plant annexins. The crystal structure of calcium-bound cotton annexin Gh1 was solved at 2.5 A resolution and shows three metal ions coordinated in the first and fourth repeat in types II and III binding sites. Although the protein has no detectable affinity for calcium in solution, in the presence of phospholipid vesicles, we determined a stoichiometry of four calcium ions per protein molecule using isothermal titration calorimetry. Further analysis of the crystal structure showed that binding of a fourth calcium ion is structurally possible in the DE loop of the first repeat. Data from this study are in agreement with the canonical membrane binding of annexins, which is facilitated by the convex surface associating with the phospholipid bilayer by a calcium bridging mechanism. In annexin Gh1, this membrane-binding state is characterized by four calcium bridges in the I/IV module of the protein and by direct interactions of several surface-exposed basic and hydrophobic residues with the phospholipid membrane. Analysis of the protein fold stability revealed that the presence of calcium lowers the thermal stability of plant annexins. Furthermore, an additional unfolding step was detected at lower temperatures, which can be explained by the anchoring of the N-terminal domain to the C-terminal core by two conserved hydrogen bonds.
The crystal structure of calcium-bound annexin Gh1 from Gossypium hirsutum and its implications for membrane binding mechanisms of plant annexins.,Hu NJ, Yusof AM, Winter A, Osman A, Reeve AK, Hofmann A J Biol Chem. 2008 Jun 27;283(26):18314-22. Epub 2008 Apr 25. PMID:18441010<ref>PMID:18441010</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Annexin|Annexin]]
*[[Annexin 3D structures|Annexin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Gossypium hirsutum]]
[[Category: Gossypium hirsutum]]
[[Category: Hofmann, A.]]
[[Category: Large Structures]]
[[Category: Hu, N J.]]
[[Category: Hofmann A]]
[[Category: Annexin]]
[[Category: Hu N-J]]
[[Category: Calcium binding]]
[[Category: Membrane binding]]
[[Category: Membrane protein]]

Latest revision as of 17:03, 13 March 2024

Crystal Structure of calcium-bound cotton annexin Gh1Crystal Structure of calcium-bound cotton annexin Gh1

Structural highlights

3brx is a 1 chain structure with sequence from Gossypium hirsutum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ANX1_GOSHI Binds to phospholipid vesicles in a calcium-dependent manner in vitro (PubMed:16331990, PubMed:18441010). Prefers phosphatidyl-serine containing membranes. May have a role in the membrane cytoskeleton scaffolding or exocytotic processes (PubMed:16331990). May be involved in oxidative stress response (Probable).[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Dabitz N, Hu NJ, Yusof AM, Tranter N, Winter A, Daley M, Zschornig O, Brisson A, Hofmann A. Structural determinants for plant annexin-membrane interactions. Biochemistry. 2005 Dec 13;44(49):16292-300. doi: 10.1021/bi0516226. PMID:16331990 doi:http://dx.doi.org/10.1021/bi0516226
  2. ↑ Hu NJ, Yusof AM, Winter A, Osman A, Reeve AK, Hofmann A. The crystal structure of calcium-bound annexin Gh1 from Gossypium hirsutum and its implications for membrane binding mechanisms of plant annexins. J Biol Chem. 2008 Jun 27;283(26):18314-22. Epub 2008 Apr 25. PMID:18441010 doi:10.1074/jbc.M801051200
  3. ↑ Hofmann A, Delmer DP, Wlodawer A. The crystal structure of annexin Gh1 from Gossypium hirsutum reveals an unusual S3 cluster. Eur J Biochem. 2003 Jun;270(12):2557-64. PMID:12787021

3brx, resolution 2.50Å

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