1n00: Difference between revisions
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< | ==Annexin Gh1 from cotton== | ||
<StructureSection load='1n00' size='340' side='right'caption='[[1n00]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1n00]] 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=1N00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N00 FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=1n00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n00 OCA], [https://pdbe.org/1n00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n00 RCSB], [https://www.ebi.ac.uk/pdbsum/1n00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n00 ProSAT]</span></td></tr> | |||
</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 == | |||
[[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/n0/1n00_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=1n00 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The three-dimensional crystal structure of recombinant annexin Gh1 from Gossypium hirsutum (cotton fibre) has been determined and refined to the final R-factor of 0.219 at the resolution of 2.1 A. This plant annexin consists of the typical 'annexin fold' and is similar to the previously solved bell pepper annexin Anx24(Ca32), but significant differences are seen when compared to the structure of nonplant annexins. A comparison with the structure of the mammalian annexin AnxA5 indicates that canonical calcium binding is geometrically possible within the membrane loops in domains I and II of Anx(Gh1) in their present conformation. All plant annexins possess a conserved tryptophan residue in the AB loop of the first domain; this residue was found to adopt both a loop-in and a loop-out conformation in the bell pepper annexin Anx24(Ca32). In Anx(Gh1), the conserved tryptophan residue is in a surface-exposed position, half way between both conformations observed in Anx24(Ca32). The present structure reveals an unusual sulfur cluster formed by two cysteines and a methionine in domains II and III, respectively. While both cysteines adopt the reduced thiolate forms and are separated by a distance of about 5.5 A, the sulfur atom of the methionine residue is in their close vicinity and apparently interacts with both cysteine sulfur atoms. While the cysteine residues are conserved in at least five plant annexins and in several mammalian members of the annexin family of proteins, the methionine residue is conserved only in three plant proteins. Several of these annexins carrying the conserved residues have been implicated in oxidative stress response. We therefore hypothesize that the cysteine motif found in the present structure, or possibly even the entire sulfur cluster, forms the molecular basis for annexin function in oxidative stress response. | |||
The crystal structure of annexin Gh1 from Gossypium hirsutum reveals an unusual S3 cluster.,Hofmann A, Delmer DP, Wlodawer A Eur J Biochem. 2003 Jun;270(12):2557-64. PMID:12787021<ref>PMID:12787021</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1n00" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Annexin 3D structures|Annexin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Gossypium hirsutum]] | [[Category: Gossypium hirsutum]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Delmer DP]] | ||
[[Category: | [[Category: Hofmann A]] | ||
[[Category: | [[Category: Wlodawer A]] | ||
Latest revision as of 11:51, 22 May 2024
Annexin Gh1 from cottonAnnexin Gh1 from cotton
Structural highlights
FunctionANX1_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. Publication Abstract from PubMedThe three-dimensional crystal structure of recombinant annexin Gh1 from Gossypium hirsutum (cotton fibre) has been determined and refined to the final R-factor of 0.219 at the resolution of 2.1 A. This plant annexin consists of the typical 'annexin fold' and is similar to the previously solved bell pepper annexin Anx24(Ca32), but significant differences are seen when compared to the structure of nonplant annexins. A comparison with the structure of the mammalian annexin AnxA5 indicates that canonical calcium binding is geometrically possible within the membrane loops in domains I and II of Anx(Gh1) in their present conformation. All plant annexins possess a conserved tryptophan residue in the AB loop of the first domain; this residue was found to adopt both a loop-in and a loop-out conformation in the bell pepper annexin Anx24(Ca32). In Anx(Gh1), the conserved tryptophan residue is in a surface-exposed position, half way between both conformations observed in Anx24(Ca32). The present structure reveals an unusual sulfur cluster formed by two cysteines and a methionine in domains II and III, respectively. While both cysteines adopt the reduced thiolate forms and are separated by a distance of about 5.5 A, the sulfur atom of the methionine residue is in their close vicinity and apparently interacts with both cysteine sulfur atoms. While the cysteine residues are conserved in at least five plant annexins and in several mammalian members of the annexin family of proteins, the methionine residue is conserved only in three plant proteins. Several of these annexins carrying the conserved residues have been implicated in oxidative stress response. We therefore hypothesize that the cysteine motif found in the present structure, or possibly even the entire sulfur cluster, forms the molecular basis for annexin function in oxidative stress response. The crystal structure of annexin Gh1 from Gossypium hirsutum reveals an unusual S3 cluster.,Hofmann A, Delmer DP, Wlodawer A Eur J Biochem. 2003 Jun;270(12):2557-64. PMID:12787021[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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