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< | ==crystal structure of Cryptosporidium parvum 14-3-3 protein in complex with peptide== | ||
<StructureSection load='2npm' size='340' side='right'caption='[[2npm]], [[Resolution|resolution]] 2.52Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2npm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptosporidium_parvum Cryptosporidium parvum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NPM 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]] 2.52Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=2npm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2npm OCA], [https://pdbe.org/2npm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2npm RCSB], [https://www.ebi.ac.uk/pdbsum/2npm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2npm ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5CUW0_CRYPI Q5CUW0_CRYPI] | |||
== 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/np/2npm_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2npm ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The parasite Cryptosporidium parvum has three 14-3-3 proteins: Cp14epsilon, Cp14a and Cp14b, with only Cp14epsilon similar to human 14-3-3 proteins in sequence, peptide-binding properties and structure. Structurally, Cp14a features the classical 14-3-3 dimer but with a uniquely wide pocket and a disoriented RRY triad potentially incapable of binding phosphopeptides. The Cp14b protein deviates from the norm significantly: (i) In one subunit, the phosphorylated C-terminal tail is bound in the binding groove like a phosphopeptide. This supports our binding study indicating this protein was stabilized by a peptide mimicking its last six residues. (ii) The other subunit has eight helices instead of nine, with alphaA and alphaB forming a single helix and occluding the peptide-binding cleft. (iii) The protein forms a degenerate dimer with the two binding grooves divided and facing opposite directions. These features conspire to block and disrupt the bicameral substrate-binding pocket, suggesting a possible tripartite auto-regulation mechanism that has not been observed previously. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1. | |||
Characterization of 14-3-3 proteins from Cryptosporidium parvum.,Brokx SJ, Wernimont AK, Dong A, Wasney GA, Lin YH, Lew J, Vedadi M, Lee WH, Hui R PLoS One. 2011;6(8):e14827. Epub 2011 Aug 11. PMID:21853016<ref>PMID:21853016</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2npm" style="background-color:#fffaf0;"></div> | |||
== References == | |||
= | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cryptosporidium parvum]] | [[Category: Cryptosporidium parvum]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arrowsmith CH]] | ||
[[Category: | [[Category: Bochkarev A]] | ||
[[Category: | [[Category: Brokx S]] | ||
[[Category: Dong A]] | |||
[[Category: Doyle D]] | |||
[[Category: Edwards AM]] | |||
[[Category: Hassanali A]] | |||
[[Category: Hui R]] | |||
[[Category: Koeieradzki I]] | |||
[[Category: Lew J]] | |||
[[Category: Lin L]] | |||
[[Category: Qiu W]] | |||
[[Category: Ren H]] | |||
[[Category: Sundstrom M]] | |||
[[Category: Vedadi M]] | |||
[[Category: Wasney G]] | |||
[[Category: Weigelt J]] | |||
[[Category: Zhao Y]] | |||
Latest revision as of 04:14, 21 November 2024
crystal structure of Cryptosporidium parvum 14-3-3 protein in complex with peptidecrystal structure of Cryptosporidium parvum 14-3-3 protein in complex with peptide
Structural highlights
FunctionEvolutionary 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 parasite Cryptosporidium parvum has three 14-3-3 proteins: Cp14epsilon, Cp14a and Cp14b, with only Cp14epsilon similar to human 14-3-3 proteins in sequence, peptide-binding properties and structure. Structurally, Cp14a features the classical 14-3-3 dimer but with a uniquely wide pocket and a disoriented RRY triad potentially incapable of binding phosphopeptides. The Cp14b protein deviates from the norm significantly: (i) In one subunit, the phosphorylated C-terminal tail is bound in the binding groove like a phosphopeptide. This supports our binding study indicating this protein was stabilized by a peptide mimicking its last six residues. (ii) The other subunit has eight helices instead of nine, with alphaA and alphaB forming a single helix and occluding the peptide-binding cleft. (iii) The protein forms a degenerate dimer with the two binding grooves divided and facing opposite directions. These features conspire to block and disrupt the bicameral substrate-binding pocket, suggesting a possible tripartite auto-regulation mechanism that has not been observed previously. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1. Characterization of 14-3-3 proteins from Cryptosporidium parvum.,Brokx SJ, Wernimont AK, Dong A, Wasney GA, Lin YH, Lew J, Vedadi M, Lee WH, Hui R PLoS One. 2011;6(8):e14827. Epub 2011 Aug 11. PMID:21853016[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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