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PDBsum entry 2ko3
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Signaling protein
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PDB id
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2ko3
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Contents |
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* Residue conservation analysis
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Febs Lett
583:3323-3328
(2009)
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PubMed id:
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60th residues of ubiquitin and Nedd8 are located out of E2-binding surfaces, but are important for K48 ubiquitin-linkage.
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Y.S.Choi,
Y.H.Jeon,
K.S.Ryu,
C.Cheong.
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ABSTRACT
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Nedd8, a ubiquitin-like modifier, is covalently attached to various proteins.
Although Nedd8 has higher sequence identity (57%) with ubiquitin, its conserved
K48 residue cannot form covalent linkage with ubiquitin. To decipher the reason
why Nedd8 cannot be an effective ubiquitin-acceptor, we compared the
non-covalent interaction between Nedd8 and ubiquitin for various E2s using
cross-saturation NMR technique. However, both Nedd8 and ubiquitin displayed
almost identical non-covalent E2-binding properties. The K60 of Nedd8 was not
present at the E2-binding surface, but its mutation to Asn converted Nedd8 into
a ubiquitin-acceptor. The N60 ubiquitin mutants also displayed a decreased
ubiquitin-accepting activity. These results suggest the presence of an
uncharacterized determinant for the K48 ubiquitin-linkage that is not related to
non-covalent E2-bindings.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.M.Wenzel,
K.E.Stoll,
and
R.E.Klevit
(2010).
E2s: structurally economical and functionally replete.
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Biochem J,
433,
31-42.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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