View source for 3oyo


==Crystal structure of hemopexin fold protein CP4 from cow pea==
<StructureSection load='3oyo' size='340' side='right'caption='[[3oyo]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3oyo]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3OYO 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]] 2.1&#8491;</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=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'>[https://proteopedia.org/fgij/fg.htm?mol=3oyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oyo OCA], [https://pdbe.org/3oyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oyo RCSB], [https://www.ebi.ac.uk/pdbsum/3oyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oyo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F2Z290_VIGUN F2Z290_VIGUN] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3oyo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vigna unguiculata]]
[[Category: Chanana V]]
[[Category: Gaur V]]
[[Category: Salunke DM]]