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1eq3

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NMR STRUCTURE OF HUMAN PARVULIN HPAR14

Structural highlights

1eq3 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PIN4_HUMAN Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.^[1] Isoform 2 binds to double-stranded DNA.^[2]

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 PubMed

The 131-amino acid residue parvulin-like human peptidyl-prolyl cis/trans isomerase (PPIase) hPar14 was shown to exhibit sequence similarity to the regulator enzyme for cell cycle transitions human hPin1, but specificity for catalyzing pSer(Thr)-Pro cis/trans isomerizations was lacking. To determine the solution structure of hPar14 the (1)H, (13)C, and (15)N chemical shifts of this protein have been assigned using heteronuclear two and three-dimensional NMR experiments on unlabeled and uniformly (15)N/(13)C-labeled recombinant protein isolated from Escherichia coli cells that overexpress the protein. The chemical shift assignments were used to interpret the NOE data, which resulted in a total of 1042 NOE restraints. The NOE restraints were used along with 71 dihedral angle restraints and 38 hydrogen bonding restraints to produce 50 low-energy structures. The hPar14 folds into a betaalpha(3)betaalphabeta(2) structure, and contains an unstructured 35-amino acid basic tail N-terminal to the catalytic core that replaces the WW domain of hPin1 homologs. The three-dimensional structures of hPar14 and the PPIase domain of human hPin1 reveal a high degree of conservation. The root-mean-square deviations of the mean atomic coordinates of the heavy atoms of the backbone between residues 38 to 45, 50 to 58, 64 to 70, 81 to 86, 115 to 119 and 122 to 128 of hPar14 were 0.81(+/-0.07) A. The hPar14 model structure provides insight into how this class of PPIases may select preferential secondary catalytic sites, and also allows identification of a putative DNA-binding motif in parvulin-like PPIases.

NMR 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.,Sekerina E, Rahfeld JU, Muller J, Fanghanel J, Rascher C, Fischer G, Bayer P J Mol Biol. 2000 Aug 25;301(4):1003-17. PMID:10966801^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fujiyama-Nakamura S, Yoshikawa H, Homma K, Hayano T, Tsujimura-Takahashi T, Izumikawa K, Ishikawa H, Miyazawa N, Yanagida M, Miura Y, Shinkawa T, Yamauchi Y, Isobe T, Takahashi N. Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage. Mol Cell Proteomics. 2009 Jul;8(7):1552-65. Epub 2009 Apr 14. PMID:19369196 doi:http://dx.doi.org/M900147-MCP200
↑ Fujiyama-Nakamura S, Yoshikawa H, Homma K, Hayano T, Tsujimura-Takahashi T, Izumikawa K, Ishikawa H, Miyazawa N, Yanagida M, Miura Y, Shinkawa T, Yamauchi Y, Isobe T, Takahashi N. Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage. Mol Cell Proteomics. 2009 Jul;8(7):1552-65. Epub 2009 Apr 14. PMID:19369196 doi:http://dx.doi.org/M900147-MCP200
↑ Sekerina E, Rahfeld JU, Muller J, Fanghanel J, Rascher C, Fischer G, Bayer P. NMR 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. J Mol Biol. 2000 Aug 25;301(4):1003-17. PMID:10966801 doi:10.1006/jmbi.2000.4013

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1eq3"

@@ Line 1: / Line 1: @@
 ==NMR STRUCTURE OF HUMAN PARVULIN HPAR14==
-<StructureSection load='1eq3' size='340' side='right'caption='[[1eq3]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
+<StructureSection load='1eq3' size='340' side='right'caption='[[1eq3]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1eq3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EQ3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1eq3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EQ3 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;'>[[1pin|1pin]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1eq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq3 OCA], [https://pdbe.org/1eq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eq3 RCSB], [https://www.ebi.ac.uk/pdbsum/1eq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eq3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PIN4_HUMAN PIN4_HUMAN]] Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.<ref>PMID:19369196</ref>   Isoform 2 binds to double-stranded DNA.<ref>PMID:19369196</ref>
+[https://www.uniprot.org/uniprot/PIN4_HUMAN PIN4_HUMAN] Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.<ref>PMID:19369196</ref>   Isoform 2 binds to double-stranded DNA.<ref>PMID:19369196</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bayer, P]]
+[[Category: Bayer P]]
-[[Category: Fischer, G]]
+[[Category: Fischer G]]
-[[Category: Muller, J]]
+[[Category: Muller J]]
-[[Category: Rahfeld, U J]]
+[[Category: Rahfeld UJ]]
-[[Category: Sekerina, E]]
+[[Category: Sekerina E]]
-[[Category: Isomerase]]
-[[Category: Parvulin]]
-[[Category: Peptidyl-prolyl cis-trans isomerase]]

1eq3

From Proteopedia

Current revision

NMR STRUCTURE OF HUMAN PARVULIN HPAR14

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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