4jp7: Difference between revisions
New page: '''Unreleased structure''' The entry 4jp7 is ON HOLD Authors: Wohlkonig, A., Wintjens, R. Description: High resolution structure of a papaya barwin-like protein (crystal form 2) |
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The | ==High resolution structure of a papaya barwin-like protein (crystal form 2)== | ||
<StructureSection load='4jp7' size='340' side='right'caption='[[4jp7]], [[Resolution|resolution]] 1.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jp7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Carica_papaya Carica papaya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JP7 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]] 1.05Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=4jp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jp7 OCA], [https://pdbe.org/4jp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jp7 RCSB], [https://www.ebi.ac.uk/pdbsum/4jp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jp7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/U5HK42_CARPA U5HK42_CARPA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The first crystal structure of a barwin-like protein, named carwin, has been determined at high resolution by single-wavelength anomalous diffraction (SAD) phasing using the six intrinsic S atoms present in the protein. The barwin-like protein was purified from Carica papaya latex and crystallized in the orthorhombic space group P212121. Using in-house Cu Kalpha X-ray radiation, 16 cumulative diffraction data sets were acquired to increase the signal-to-noise level and thereby the anomalous scattering signal. A sequence-database search on the papaya genome identified two carwin isoforms of 122 residues in length, both containing six S atoms that yield an estimated Bijvoet ratio of 0.93% at 1.54 A wavelength. A systematic analysis of data quality and redundancy was performed to assess the capacity to locate the S atoms and to phase the data. It was observed that the crystal decay was low during data collection and that successful S-SAD phasing could be obtained with a relatively low data multiplicity of about 7. Using a synchrotron source, high-resolution data (1 A) were collected from two different crystal forms of the papaya latex carwin. The refined structures showed a central beta-barrel of six strands surrounded by several alpha-helices and loops. The beta-barrel of carwin appears to be a common structural module that is shared within several other unrelated proteins. Finally, the possible biological function of the protein is discussed. | |||
High-resolution structure of a papaya plant-defence barwin-like protein solved by in-house sulfur-SAD phasing.,Huet J, Teinkela Mbosso EJ, Soror S, Meyer F, Looze Y, Wintjens R, Wohlkonig A Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):2017-26. doi:, 10.1107/S0907444913018015. Epub 2013 Sep 20. PMID:24100320<ref>PMID:24100320</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4jp7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Carica papaya]] | |||
[[Category: Large Structures]] | |||
[[Category: Wintjens R]] | |||
[[Category: Wohlkonig A]] | |||
Latest revision as of 09:38, 17 October 2024
High resolution structure of a papaya barwin-like protein (crystal form 2)High resolution structure of a papaya barwin-like protein (crystal form 2)
Structural highlights
FunctionPublication Abstract from PubMedThe first crystal structure of a barwin-like protein, named carwin, has been determined at high resolution by single-wavelength anomalous diffraction (SAD) phasing using the six intrinsic S atoms present in the protein. The barwin-like protein was purified from Carica papaya latex and crystallized in the orthorhombic space group P212121. Using in-house Cu Kalpha X-ray radiation, 16 cumulative diffraction data sets were acquired to increase the signal-to-noise level and thereby the anomalous scattering signal. A sequence-database search on the papaya genome identified two carwin isoforms of 122 residues in length, both containing six S atoms that yield an estimated Bijvoet ratio of 0.93% at 1.54 A wavelength. A systematic analysis of data quality and redundancy was performed to assess the capacity to locate the S atoms and to phase the data. It was observed that the crystal decay was low during data collection and that successful S-SAD phasing could be obtained with a relatively low data multiplicity of about 7. Using a synchrotron source, high-resolution data (1 A) were collected from two different crystal forms of the papaya latex carwin. The refined structures showed a central beta-barrel of six strands surrounded by several alpha-helices and loops. The beta-barrel of carwin appears to be a common structural module that is shared within several other unrelated proteins. Finally, the possible biological function of the protein is discussed. High-resolution structure of a papaya plant-defence barwin-like protein solved by in-house sulfur-SAD phasing.,Huet J, Teinkela Mbosso EJ, Soror S, Meyer F, Looze Y, Wintjens R, Wohlkonig A Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):2017-26. doi:, 10.1107/S0907444913018015. Epub 2013 Sep 20. PMID:24100320[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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