1e0q

From Proteopedia

(Difference between revisions)

Current revision

Mutant Peptide from the first N-terminal 17 amino-acid of Ubiquitin

Structural highlights

1e0q is a 1 chain structure with sequence from Bos taurus. 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

UBB_BOVIN Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).

Publication Abstract from PubMed

The formation of the N-terminal beta-hairpin of ubiquitin is thought to be an early event in the folding of this small protein. Previously, we have shown that a peptide corresponding to residues 1-17 of ubiquitin folds autonomously and is likely to have a native-like hairpin register. To investigate the causes of the stability of this fold, we have made mutations in the amino acids at the apex of the turn. We find that in a peptide where Thr9 is replaced by Asp, U(1-17)T9D, the native conformation is stabilized with respect to the wild-type sequence, so much so that we are able to characterize the structure of the mutant peptide fully by NMR spectroscopy. The data indicate that U(1-17)T9D peptide does indeed form a hairpin with a native-like register and a type I turn with a G1 beta-bulge, as in the full-length protein. The reason for the greater stability of the U(1-17)T9D mutant remains uncertain, but there are nuclear Overhauser effects between the side chains of Asp9 and Lys 11, which may indicate that a charge-charge interaction between these residues is responsible.

Structural characterization of a mutant peptide derived from ubiquitin: implications for protein folding.,Zerella R, Chen PY, Evans PA, Raine A, Williams DH Protein Sci. 2000 Nov;9(11):2142-50. PMID:11152124^[1]

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

References

↑ Zerella R, Chen PY, Evans PA, Raine A, Williams DH. Structural characterization of a mutant peptide derived from ubiquitin: implications for protein folding. Protein Sci. 2000 Nov;9(11):2142-50. PMID:11152124

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e0q"

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1e0q.png|left|200px]]
-<!--
+==Mutant Peptide from the first N-terminal 17 amino-acid of Ubiquitin==
-The line below this paragraph, containing "STRUCTURE_1e0q", creates the "Structure Box" on the page.
+<StructureSection load='1e0q' size='340' side='right'caption='[[1e0q]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1e0q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E0Q FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=1e0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0q OCA], [https://pdbe.org/1e0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e0q RCSB], [https://www.ebi.ac.uk/pdbsum/1e0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0q ProSAT]</span></td></tr>
-{{STRUCTURE_1e0q|  PDB=1e0q  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/UBB_BOVIN UBB_BOVIN] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The formation of the N-terminal beta-hairpin of ubiquitin is thought to be an early event in the folding of this small protein. Previously, we have shown that a peptide corresponding to residues 1-17 of ubiquitin folds autonomously and is likely to have a native-like hairpin register. To investigate the causes of the stability of this fold, we have made mutations in the amino acids at the apex of the turn. We find that in a peptide where Thr9 is replaced by Asp, U(1-17)T9D, the native conformation is stabilized with respect to the wild-type sequence, so much so that we are able to characterize the structure of the mutant peptide fully by NMR spectroscopy. The data indicate that U(1-17)T9D peptide does indeed form a hairpin with a native-like register and a type I turn with a G1 beta-bulge, as in the full-length protein. The reason for the greater stability of the U(1-17)T9D mutant remains uncertain, but there are nuclear Overhauser effects between the side chains of Asp9 and Lys 11, which may indicate that a charge-charge interaction between these residues is responsible.
-===MUTANT PEPTIDE FROM THE FIRST N-TERMINAL 17 AMINO-ACID OF UBIQUITIN===
+Structural characterization of a mutant peptide derived from ubiquitin: implications for protein folding.,Zerella R, Chen PY, Evans PA, Raine A, Williams DH Protein Sci. 2000 Nov;9(11):2142-50. PMID:11152124<ref>PMID:11152124</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1e0q" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_11152124}}, adds the Publication Abstract to the page
+*[[3D structures of ubiquitin|3D structures of ubiquitin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 11152124 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11152124}}
+__TOC__
+</StructureSection>
-==About this Structure==
-E0Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0Q OCA].
-==Reference==
-Structural characterization of a mutant peptide derived from ubiquitin: implications for protein folding., Zerella R, Chen PY, Evans PA, Raine A, Williams DH, Protein Sci. 2000 Nov;9(11):2142-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11152124 11152124]
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Chen, P Y.]]
+[[Category: Chen PY]]
-[[Category: Evans, P A.]]
+[[Category: Evans PA]]
-[[Category: Raine, A.]]
+[[Category: Raine A]]
-[[Category: Williams, D H.]]
+[[Category: Williams DH]]
-[[Category: Zerella, R.]]
+[[Category: Zerella R]]
-[[Category: Hairpin]]
-[[Category: Mutant peptide]]
-[[Category: Peptide]]
-[[Category: Ubiquitin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:56:49 2008''

1e0q

From Proteopedia

Current revision

Mutant Peptide from the first N-terminal 17 amino-acid of Ubiquitin

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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