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1q7s

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Revision as of 09:38, 8 September 2021

Crystal structure of bit1

Structural highlights

1q7s is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PTH2_HUMAN] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity).^[1] Promotes caspase-independent apoptosis by regulating the function of two transcriptional regulators, AES and TLE1.^[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

Peptidyl-tRNA hydrolase (Pth) activity releases tRNA from the premature translation termination product peptidyl-tRNA. Two different enzymes have been reported to encode such activity, Pth present in bacteria and eukaryotes and Pth2 present in archaea and eukaryotes. Here we report the crystallographic structure of the Homo sapiens Pth2 at a 2.0-A resolution as well as its catalytic properties. In contrast to the structure of Escherichia coli Pth, H. sapiens Pth2 has an alpha/beta fold with a four-stranded antiparallel beta-sheet in its core surrounded by two alpha-helices on each side. This arrangement of secondary structure elements generates a fold not previously reported. Its catalytic efficiency is comparable with that reported for the archaeal Sulfolobus solfataricus Pth2 and higher than that of the bacterial E. coli Pth. Several lines of evidence target the active site to two close loops with highly conserved residues. This active site architecture is unrelated to that of E. coli Pth. In addition, intermolecular contacts in the crystal asymmetric unit cell suggest a likely surface for protein-protein interactions related to the Pth2-mediated apoptosis.

Crystal structure of a human peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity.,De Pereda JM, Waas WF, Jan Y, Ruoslahti E, Schimmel P, Pascual J J Biol Chem. 2004 Feb 27;279(9):8111-5. Epub 2003 Dec 5. PMID:14660562^[3]

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

References

↑ Jan Y, Matter M, Pai JT, Chen YL, Pilch J, Komatsu M, Ong E, Fukuda M, Ruoslahti E. A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors. Cell. 2004 Mar 5;116(5):751-62. PMID:15006356
↑ Jan Y, Matter M, Pai JT, Chen YL, Pilch J, Komatsu M, Ong E, Fukuda M, Ruoslahti E. A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors. Cell. 2004 Mar 5;116(5):751-62. PMID:15006356
↑ De Pereda JM, Waas WF, Jan Y, Ruoslahti E, Schimmel P, Pascual J. Crystal structure of a human peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity. J Biol Chem. 2004 Feb 27;279(9):8111-5. Epub 2003 Dec 5. PMID:14660562 doi:10.1074/jbc.M311449200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q7s"

@@ Line 3: / Line 3: @@
 <StructureSection load='1q7s' size='340' side='right'caption='[[1q7s]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1q7s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q7S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1q7s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q7S FirstGlance]. <br>
-</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=1q7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7s OCA], [http://pdbe.org/1q7s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q7s RCSB], [http://www.ebi.ac.uk/pdbsum/1q7s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q7s ProSAT]</span></td></tr>
+</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=1q7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7s OCA], [https://pdbe.org/1q7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q7s RCSB], [https://www.ebi.ac.uk/pdbsum/1q7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q7s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PTH2_HUMAN PTH2_HUMAN]] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity).<ref>PMID:15006356</ref>   Promotes caspase-independent apoptosis by regulating the function of two transcriptional regulators, AES and TLE1.<ref>PMID:15006356</ref>
+[[https://www.uniprot.org/uniprot/PTH2_HUMAN PTH2_HUMAN]] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity).<ref>PMID:15006356</ref>   Promotes caspase-independent apoptosis by regulating the function of two transcriptional regulators, AES and TLE1.<ref>PMID:15006356</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1q7s

From Proteopedia

Revision as of 09:38, 8 September 2021

Crystal structure of bit1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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