EzCatDB: D00493

DB codeD00493
CATH domainDomain 12.20.70.10
Domain 23.10.50.40Catalytic domain
E.C.5.2.1.8
CSA1nmw


Enzyme Name
Swiss-protKEGG

Q13526
Protein namePeptidyl-prolyl cis-trans isomerase NIMA-interacting 1peptidylprolyl isomerase
PPIase
cyclophilin [misleading, see comments]
peptide bond isomerase
peptidyl-prolyl cis-trans isomerase
SynonymsEC 5.2.1.8
Rotamase Pin1
PPIase Pin1


Swiss-prot:Accession NumberQ13526
Entry namePIN1_HUMAN
ActivityPeptidylproline (omega=180) = peptidylproline (omega=0).
SubunitInteracts with STIL (By similarity). Interacts with MPHOSPH1.
Subcellular locationNucleus.
Cofactor


SubstratesProducts
KEGG-idC03798C03633
CompoundPeptidylproline (omega=180, trans)Peptidylproline (omega=0, cis)
Typeamino acids,peptide/proteinamino acids,peptide/protein
1f8aB01UnboundUnbound
1nmvA01UnboundUnbound
1pinA01UnboundUnbound
1f8aB02UnboundUnbound
1nmvA02UnboundUnbound
1nmwAUnboundUnbound
1pinA02UnboundAnalogue:ALA-PRO(chain B)

Active-site residues
resource
literature [1]
pdbCatalytic residues
1f8aB01
1nmvA01
1pinA01
1f8aB02HIS 63;CYS 117;SER 158;HIS 161
1nmvA02HIS 59;CYS 113;SER 154;HIS 157
1nmwAHIS 59;CYS 113;SER 154;HIS 157
1pinA02HIS 59;CYS 113;SER 154;HIS 157

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Fig.7, p.880-883
[3]

[28]


references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS)
Medline ID97344079
PubMed ID9200606
JournalCell
Year1997
Volume89
Pages875-86
AuthorsRanganathan R, Lu KP, Hunter T, Noel JP
TitleStructural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent.
Related PDB1pin
Related Swiss-protQ13526
[2]
PubMed ID9548941
JournalBiochemistry
Year1998
Volume37
Pages5566-75
AuthorsSchutkowski M, Bernhardt A, Zhou XZ, Shen M, Reimer U, Rahfeld JU, Lu KP, Fischer G
TitleRole of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and Pin1 substrate recognition.
[3]
PubMed ID11212339
JournalCell Mol Life Sci
Year1999
Volume56
Pages788-806
AuthorsZhou XZ, Lu PJ, Wulf G, Lu KP
TitlePhosphorylation-dependent prolyl isomerization: a novel signaling regulatory mechanism.
[4]
PubMed ID11163176
JournalCell
Year2000
Volume103
Pages1001-4
AuthorsSudol M, Hunter T
TitleNeW wrinkles for an old domain.
[5]
PubMed ID10899126
JournalEMBO J
Year2000
Volume19
Pages3727-38
AuthorsWu X, Wilcox CB, Devasahayam G, Hackett RL, Arevalo-Rodriguez M, Cardenas ME, Heitman J, Hanes SD
TitleThe Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery.
[6]
PubMed ID10744752
JournalJ Biol Chem
Year2000
Volume275
Pages10577-81
AuthorsLandrieu I, De Veylder L, Fruchart JS, Odaert B, Casteels P, Portetelle D, Van Montagu M, Inze D, Lippens G
TitleThe Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase.
[7]
PubMed ID10966801
JournalJ Mol Biol
Year2000
Volume301
Pages1003-17
AuthorsSekerina E, Rahfeld JU, Muller J, Fanghanel J, Rascher C, Fischer G, Bayer P
TitleNMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.
[8]
CommentsX-ray crystallography
PubMed ID10932246
JournalNat Struct Biol
Year2000
Volume7
Pages639-43
AuthorsVerdecia MA, Bowman ME, Lu KP, Hunter T, Noel JP
TitleStructural basis for phosphoserine-proline recognition by group IV WW domains.
Related PDB1f8a
[9]
PubMed ID10932238
JournalNat Struct Biol
Year2000
Volume7
Pages611-3
AuthorsZarrinpar A, Lim WA
TitleConverging on proline: the mechanism of WW domain peptide recognition.
[10]
PubMed ID11456485
JournalBiochemistry
Year2001
Volume40
Pages8479-86
AuthorsMyers JK, Morris DP, Greenleaf AL, Oas TG
TitlePhosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1.
[11]
PubMed ID11795843
JournalCurr Genet
Year2001
Volume40
Pages234-42
AuthorsWu X, Chang A, Sudol M, Hanes SD
TitleGenetic interactions between the ESS1 prolyl-isomerase and the RSP5 ubiquitin ligase reveal opposing effects on RNA polymerase II function.
[12]
PubMed ID11223034
JournalFEBS Lett
Year2001
Volume490
Pages190-5
AuthorsSudol M, Sliwa K, Russo T
TitleFunctions of WW domains in the nucleus.
[13]
PubMed ID11470801
JournalJ Biol Chem
Year2001
Volume276
Pages37520-8
AuthorsKamimoto T, Zama T, Aoki R, Muro Y, Hagiwara M
TitleIdentification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1.
[14]
PubMed ID11013245
JournalJ Biol Chem
Year2001
Volume276
Pages1434-8
AuthorsLandrieu I, Odaert B, Wieruszeski JM, Drobecq H, Rousselot-Pailley P, Inze D, Lippens G
Titlep13(SUC1) and the WW domain of PIN1 bind to the same phosphothreonine-proline epitope.
[15]
PubMed ID11118437
JournalJ Biol Chem
Year2001
Volume276
Pages13524-9
AuthorsMetzner M, Stoller G, Rucknagel KP, Lu KP, Fischer G, Luckner M, Kullertz G
TitleFunctional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13.
[16]
PubMed ID11313338
JournalJ Biol Chem
Year2001
Volume276
Pages25150-6
AuthorsWintjens R, Wieruszeski JM, Drobecq H, Rousselot-Pailley P, Buee L, Lippens G, Landrieu I
Title1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides.
[17]
PubMed ID11118438
JournalJ Biol Chem
Year2001
Volume276
Pages13517-23
AuthorsYao JL, Kops O, Lu PJ, Lu KP
TitleFunctional conservation of phosphorylation-specific prolyl isomerases in plants.
[18]
PubMed ID11389853
JournalMol Cell
Year2001
Volume7
Pages1071-83
AuthorsStukenberg PT, Kirschner MW
TitlePin1 acts catalytically to promote a conformational change in Cdc25.
[19]
PubMed ID11786999
JournalBiopolymers
Year2002
Volume63
Pages111-21
AuthorsKowalski JA, Liu K, Kelly JW
TitleNMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1.
[20]
PubMed ID11904169
JournalFEBS Lett
Year2002
Volume513
Pages305-11
AuthorsKops O, Zhou XZ, Lu KP
TitlePin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1.
[21]
PubMed ID11982361
JournalJ Am Chem Soc
Year2002
Volume124
Pages4980-6
AuthorsDeechongkit S, Kelly JW
TitleThe effect of backbone cyclization on the thermodynamics of beta-sheet unfolding: stability optimization of the PIN WW domain.
[22]
PubMed ID12358534
JournalJ Am Chem Soc
Year2002
Volume124
Pages11900-7
AuthorsKaul R, Deechongkit S, Kelly JW
TitleSynthesis of a negatively charged dibenzofuran-based beta-turn mimetic and its incorporation into the WW miniprotein-enhanced solubility without a loss of thermodynamic stability.
[23]
PubMed ID11751914
JournalJ Biol Chem
Year2002
Volume277
Pages10173-7
AuthorsKato Y, Ito M, Kawai K, Nagata K, Tanokura M
TitleDeterminants of ligand specificity in groups I and IV WW domains as studied by surface plasmon resonance and model building.
[24]
PubMed ID11723108
JournalJ Biol Chem
Year2002
Volume277
Pages2381-4
AuthorsLu PJ, Zhou XZ, Liou YC, Noel JP, Lu KP
TitleCritical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function.
[25]
PubMed ID12153046
JournalJ Biomol NMR
Year2002
Volume23
Pages163-4
AuthorsJacobs DM, Saxena K, Grimme S, Vogtherr M, Pescatore B, Langer T, Elshorst B, Fiebig KM
Title1H, 13C and 15N backbone resonance assignment of the peptidyl-prolyl cis-trans isomerase Pin1.
[26]
PubMed ID12079389
JournalJ Mol Biol
Year2002
Volume320
Pages321-32
AuthorsLandrieu I, Wieruszeski JM, Wintjens R, Inze D, Lippens G
TitleSolution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana.
Related PDB1j6y
[27]
PubMed ID12397361
JournalNature
Year2002
Volume419
Pages849-53
AuthorsZheng H, You H, Zhou XZ, Murray SA, Uchida T, Wulf G, Gu L, Tang X, Lu KP, Xiao ZX
TitleThe prolyl isomerase Pin1 is a regulator of p53 in genotoxic response.
[28]
CommentsNMR structure
PubMed ID12721297
JournalJ Biol Chem
Year2003
Volume278
Pages26183-93
AuthorsBayer E, Goettsch S, Mueller JW, Griewel B, Guiberman E, Mayr LM, Bayer P
TitleStructural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding.
Related PDB1nmv,1nmw
[29]
PubMed ID12686540
JournalJ Biol Chem
Year2003
Volume278
Pages26174-82
AuthorsJacobs DM, Saxena K, Vogtherr M, Bernado P, Pons M, Fiebig KM
TitlePeptide binding induces large scale changes in inter-domain mobility in human Pin1.
[30]
PubMed ID12471608
JournalProteins
Year2003
Volume50
Pages158-69
AuthorsWang T, Wade RC
TitleImplicit solvent models for flexible protein-protein docking by molecular dynamics simulation.
[31]
PubMed ID15229605
JournalNature
Year2004
Volume430
Pages101-5
AuthorsDeechongkit S, Nguyen H, Powers ET, Dawson PE, Gruebele M, Kelly JW
TitleContext-dependent contributions of backbone hydrogen bonding to beta-sheet folding energetics.

comments
According to the literature [1], this enzyme catalyzes the following reactions:
(A) Addition of Cys to carbonyl carbon of substrate, leading to a formation of tetrahedral intermediate.
(B) Elimination of Cys from the tetrahedral intermediate.

createdupdated
2005-05-062009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.