View source for 4lzi


==Characterization of Solanum tuberosum Multicystatin and Significance of Core Domains==
<StructureSection load='4lzi' size='340' side='right'caption='[[4lzi]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lzi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LZI 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]] 2.2&#8491;</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=4lzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lzi OCA], [https://pdbe.org/4lzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lzi RCSB], [https://www.ebi.ac.uk/pdbsum/4lzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lzi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYTM_SOLTU CYTM_SOLTU] Probably has a role in the plant's defense system.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Potato (Solanum tuberosum) multicystatin (PMC) is a unique cystatin composed of eight repeating units, each capable of inhibiting cysteine proteases. PMC is a composite of several cystatins linked by trypsin-sensitive (serine protease) domains and undergoes transitions between soluble and crystalline forms. However, the significance and the regulatory mechanism or mechanisms governing these transitions are not clearly established. Here, we report the 2.2-A crystal structure of the trypsin-resistant PMC core consisting of the fifth, sixth, and seventh domains. The observed interdomain interaction explains PMC's resistance to trypsin and pH-dependent solubility/aggregation. Under acidic pH, weakening of the interdomain interactions exposes individual domains, resulting in not only depolymerization of the crystalline form but also exposure of cystatin domains for inhibition of cysteine proteases. This in turn allows serine protease-mediated fragmentation of PMC, producing approximately 10-kD domains with intact inhibitory capacity and faster diffusion, thus enhancing PMC's inhibitory ability toward cysteine proteases. The crystal structure, light-scattering experiments, isothermal titration calorimetry, and site-directed mutagenesis confirmed the critical role of pH and N-terminal residues in these dynamic transitions between monomer/polymer of PMC. Our data support a notion that the pH-dependent structural regulation of PMC has defense-related implications in tuber physiology via its ability to regulate protein catabolism.

Characterization of Solanum tuberosum Multicystatin and the Significance of Core Domains.,Green AR, Nissen MS, Kumar GN, Knowles NR, Kang C Plant Cell. 2013 Dec;25(12):5043-52. doi: 10.1105/tpc.113.121004. Epub 2013 Dec, 20. PMID:24363310<ref>PMID:24363310</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4lzi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Solanum tuberosum]]
[[Category: Green AR]]
[[Category: Kang C]]
[[Category: Knowles NR]]
[[Category: Kumar GN]]
[[Category: Nissen MS]]