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| | <StructureSection load='3rnz' size='340' side='right'caption='[[3rnz]], [[Resolution|resolution]] 2.01Å' scene=''> | | <StructureSection load='3rnz' size='340' side='right'caption='[[3rnz]], [[Resolution|resolution]] 2.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rnz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. 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> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ro0|3ro0]], [[3ro1|3ro1]]</div></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]] 2.01Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcp ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 "Bacillus amyloliquifaciens" (sic) Fukumoto 1943])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pyroglutamyl-peptidase_I Pyroglutamyl-peptidase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.3 3.4.19.3] </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=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> | | <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> | | </table> |
| | == Function == | | == 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]
| + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Bacillus amyloliquefaciens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pyroglutamyl-peptidase I]]
| + | [[Category: Lo Y-C]] |
| - | [[Category: Lo, Y C]] | + | [[Category: Wang AH-J]] |
| - | [[Category: Wang, A H.J]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
PCP_BACAM Removes 5-oxoproline from various penultimate amino acid residues except L-proline.[HAMAP-Rule:MF_00417]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lo YC, Su WC, Ko TP, Wang NC, Wang AH. Terpyridine Platinum(II) Complexes Inhibit Cysteine Proteases by Binding to Active-site Cysteine. J Biomol Struct Dyn. 2011 Oct;29(2):267-82. PMID:21875148
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