3oyo: Difference between revisions
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==Crystal structure of hemopexin fold protein CP4 from cow pea== | |||
=== | <StructureSection load='3oyo' size='340' side='right' caption='[[3oyo]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3oyo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vigna_unguiculata Vigna unguiculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OYO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OYO FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oyo RCSB], [http://www.ebi.ac.uk/pdbsum/3oyo PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The haemopexin fold is present in almost all life forms and is utilized for carrying out diverse physiological functions. The structure of CP4, a haemopexin-fold protein from cow pea (Vigna unguiculata), was determined at 2.1 A resolution. The protein exists as a monomer both in solution and in the crystal. The structure revealed a typical four-bladed beta-propeller topology. The protein exhibits 42% sequence similarity to LS-24 from Lathyrus sativus, with substantial differences in the surface-charge distribution and in the oligomeric state. A structure-based sequence analysis of haemopexin-fold proteins of plant and mammalian origin established a sequence signature associated with the haemopexin motif. This signature sequence enabled the identification of other proteins with possible haemopexin-like topology of both plant and animal origin. Although CP4 shares a structural fold with LS-24 and other haemopexins, biochemical studies indicated possible functional differences between CP4 and LS-24. While both of these proteins exhibit spermine-binding potential, CP4 does not bind to haem, unlike LS-24. | |||
The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants.,Gaur V, Chanana V, Jain A, Salunke DM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt, 2):193-200. Epub 2011 Jan 21. PMID:21301085<ref>PMID:21301085</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Vigna unguiculata]] | [[Category: Vigna unguiculata]] | ||
[[Category: Chanana, V | [[Category: Chanana, V]] | ||
[[Category: Gaur, V | [[Category: Gaur, V]] | ||
[[Category: Salunke, D M | [[Category: Salunke, D M]] | ||
[[Category: Hemopexin]] | [[Category: Hemopexin]] | ||
[[Category: Plant protein]] | [[Category: Plant protein]] | ||
[[Category: Seed]] | [[Category: Seed]] | ||
