View source for 3rnz


==Crystal structure of Bacillus Amyloliquefaciens Pyroglutamyl Peptidase I==
<StructureSection load='3rnz' size='340' side='right'caption='[[3rnz]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3rnz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RNZ 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]] 2.01&#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=3rnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rnz OCA], [https://pdbe.org/3rnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rnz RCSB], [https://www.ebi.ac.uk/pdbsum/3rnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rnz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PCP_BACAM PCP_BACAM] Removes 5-oxoproline from various penultimate amino acid residues except L-proline.[HAMAP-Rule:MF_00417]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Platinum(II) complexes have been demonstrated to form covalent bonds with sulfur-donating ligands (in glutathione, metallothionein and other sulfur-containing biomolecules) or coordination bonds with nitrogen-donating ligands (such as histidine and guanine). To investigate how these compounds interact with cysteine proteases, we chose terpyridine platinum(II) (TP-Pt(II)) complexes as a model system. By using X-ray crystallography, we demonstrated that TP-Pt(II) formed a covalent bond with the catalytic cysteine residue in pyroglutamyl peptidase I. Moreover, by using MALDI (matrix-assisted laser desorption/ionization) and TOF-TOF (time of flight) mass spectrometry, we elucidated that the TP-Pt(II) complex formed a covalent bond with the active-site cysteine residue in two other types of cysteine protease. Taken together, the results unequivocally showed that TP-Pt(II) complexes can selectively bind to the active site of most cysteine proteases. Our findings here can be useful in the design of new anti-cancer, anti-parasite or anti-virus platinum(II) compounds.

Terpyridine Platinum(II) Complexes Inhibit Cysteine Proteases by Binding to Active-site Cysteine.,Lo YC, Su WC, Ko TP, Wang NC, Wang AH J Biomol Struct Dyn. 2011 Oct;29(2):267-82. PMID:21875148<ref>PMID:21875148</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3rnz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus amyloliquefaciens]]
[[Category: Large Structures]]
[[Category: Lo Y-C]]
[[Category: Wang AH-J]]