View source for 4hgu

==Crystal Structure of Galleria mellonella Silk Protease Inhibitor 2==
<StructureSection load='4hgu' size='340' side='right' caption='[[4hgu]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hgu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Galme Galme]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HGU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1an1|1an1]], [[2ovo|2ovo]], [[3pis|3pis]]</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=4hgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hgu RCSB], [http://www.ebi.ac.uk/pdbsum/4hgu PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Purification of suitable quantity of homogenous protein is very often the bottleneck in protein structural studies. Overexpression of a desired gene and attachment of enzymatically cleavable affinity tags to the protein of interest made a breakthrough in this field. Here we describe the structure of Galleria mellonella silk proteinase inhibitor 2 (GmSPI-2) determined both by X-ray diffraction and NMR spectroscopy methods. GmSPI-2 was purified using a new method consisting in non-enzymatic His-tag removal based on a highly specific peptide bond cleavage reaction assisted by Ni(II) ions. The X-ray crystal structure of GmSPI-2 was refined against diffraction data extending to 0.98 A resolution measured at 100 K using synchrotron radiation. Anisotropic refinement with the removal of stereochemical restraints for the well-ordered parts of the structure converged with R factor of 10.57% and Rfree of 12.91%. The 3D structure of GmSPI-2 protein in solution was solved on the basis of 503 distance constraints, 10 hydrogen bonds and 26 torsion angle restraints. It exhibits good geometry and side-chain packing parameters. The models of the protein structure obtained by X-ray diffraction and NMR spectroscopy are very similar to each other and reveal the same beta2alphabeta fold characteristic for Kazal-family serine proteinase inhibitors.

Atomic resolution structure of a protein prepared by non-enzymatic His-tag removal. Crystallographic and NMR study of GmSPI-2 inhibitor.,Kopera E, Bal W, Lenarcic Zivkovic M, Dvornyk A, Kludkiewicz B, Grzelak K, Zhukov I, Zagorski-Ostoja W, Jaskolski M, Krzywda S PLoS One. 2014 Sep 18;9(9):e106936. doi: 10.1371/journal.pone.0106936., eCollection 2014. PMID:25233114<ref>PMID:25233114</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Galme]]
[[Category: Bal, W]]
[[Category: Dvornyk, A]]
[[Category: Grzelak, K]]
[[Category: Jaskolski, M]]
[[Category: Kludkiewicz, B]]
[[Category: Kopera, E]]
[[Category: Krzywda, S]]
[[Category: Zagorski, W]]
[[Category: Hydrolase inhibitor]]
[[Category: Kazal-type serine protease inhibitor]]