View source for 4toq


==Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity==
<StructureSection load='4toq' size='340' side='right'caption='[[4toq]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4toq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Punica_granatum Punica granatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TOQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4toq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4toq OCA], [https://pdbe.org/4toq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4toq RCSB], [https://www.ebi.ac.uk/pdbsum/4toq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4toq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CHIT_PUNGR CHIT_PUNGR] Hydrolyzes chitin. Probable calcium storage protein of the seeds. Binds calcium ions with high capacity and low affinity. Involved in seed germination.<ref>PMID:21790816</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chitinase hydrolyzes the beta-1,4-glycosidic bond in chitin. In higher plants, this enzyme has been regarded as a pathogenesis-related protein. Recently, we identified a class III chitinase, which functions as a calcium storage protein in pomegranate (Punica granatum) seed (PSC, pomegranate seed chitinase). Here, we solved a crystal structure of PSC at 1.6 A resolution. Although its overall structure, including the structure of catalytic site and non-proline cis-peptides, was closely similar to those of other class III chitinases, PSC had some unique structural characteristics. First, there were some metal-binding sites with coordinated water molecules on the surface of PSC. Second, many unconserved aspartate residues were present in the PSC sequence which rendered the surface of PSC negatively charged. This acidic electrostatic property is in contrast to that of hevamine, well-characterized plant class III chitinase, which has rather a positively charged surface. Thus, the crystal structure provides a clue for metal association property of PSC.

Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity.,Masuda T, Zhao G, Mikami B Biosci Biotechnol Biochem. 2014 Sep 25:1-6. PMID:25252615<ref>PMID:25252615</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4toq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chitinase 3D structures|Chitinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Punica granatum]]
[[Category: Masuda T]]
[[Category: Mikami B]]
[[Category: Zhao G]]