4hgu: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hgu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Galleria_mellonella Galleria mellonella]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4HGU FirstGlance]. <br> | <table><tr><td colspan='2'>[[4hgu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Galleria_mellonella Galleria mellonella]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4HGU FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.98Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4hgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgu OCA], [https://pdbe.org/4hgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hgu RCSB], [https://www.ebi.ac.uk/pdbsum/4hgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hgu ProSAT]</span></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=4hgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgu OCA], [https://pdbe.org/4hgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hgu RCSB], [https://www.ebi.ac.uk/pdbsum/4hgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hgu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 18:05, 20 September 2023
Crystal Structure of Galleria mellonella Silk Protease Inhibitor 2Crystal Structure of Galleria mellonella Silk Protease Inhibitor 2
Structural highlights
FunctionPublication Abstract from PubMedPurification 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||