2df5: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2df5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DF5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2df5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DF5 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iof|1iof]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iof|1iof]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyroglutamyl-peptidase_I Pyroglutamyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.3 3.4.19.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyroglutamyl-peptidase_I Pyroglutamyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.3 3.4.19.3] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2df5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2df5 RCSB], [http://www.ebi.ac.uk/pdbsum/2df5 PDBsum]</span></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=2df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2df5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2df5 RCSB], [http://www.ebi.ac.uk/pdbsum/2df5 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PCP_PYRFU PCP_PYRFU]] Removes 5-oxoproline from various penultimate amino acid residues except L-proline.[HAMAP-Rule:MF_00417] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Pyroglutamyl-peptidase I]] | [[Category: Pyroglutamyl-peptidase I]] | ||
[[Category: Chon, H | [[Category: Chon, H]] | ||
[[Category: Kanaya, S | [[Category: Kanaya, S]] | ||
[[Category: Katagiri, Y | [[Category: Katagiri, Y]] | ||
[[Category: Koga, Y | [[Category: Koga, Y]] | ||
[[Category: Matsumura, H | [[Category: Matsumura, H]] | ||
[[Category: Takano, K | [[Category: Takano, K]] | ||
[[Category: Chameleon sequence]] | [[Category: Chameleon sequence]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Pyrrolidone carboxyl peptidase]] | [[Category: Pyrrolidone carboxyl peptidase]] | ||
Revision as of 01:12, 26 December 2014
Crystal Structure of Pf-PCP(1-204)-CCrystal Structure of Pf-PCP(1-204)-C
Structural highlights
Function[PCP_PYRFU] Removes 5-oxoproline from various penultimate amino acid residues except L-proline.[HAMAP-Rule:MF_00417] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCertain sequences, known as chameleon sequences, take both alpha- and beta-conformations in natural proteins. We demonstrate that a wild chameleon sequence fused to the C-terminal alpha-helix or beta-sheet in foreign stable proteins from hyperthermophiles forms the same conformation as the host secondary structure. However, no secondary structural formation is observed when the sequence is attached to the outside of the secondary structure. These results indicate that this sequence inherently possesses an ability to make either alpha- or beta-conformation, depending on the sequentially neighboring secondary structure if little other nonlocal interaction occurs. Thus, chameleon sequences take on a satellite state through contagion by the power of a secondary structure. We propose this "conformational contagion" as a new nonlocal determinant factor in protein structure and misfolding related to protein conformational diseases. Conformational contagion in a protein: structural properties of a chameleon sequence.,Takano K, Katagiri Y, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S Proteins. 2007 Aug 15;68(3):617-25. PMID:17510955[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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