Linked Life Data

15723523

Source:http://linkedlifedata.com/resource/pubmed/id/15723523

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2005-2-22
pubmed:databankReference
pubmed:abstractText
Small ubiquitin-related modifier SUMO-3 is a member of a growing family of ubiquitin-like proteins (Ubls). So far, four isoforms of SUMO have been identified in humans. It is generally known that SUMO modification regulates protein localization and activity. Previous structure and function studies have been mainly focused on SUMO-1. The sequence of SUMO-3 is 46% identical with that of SUMO-1; nevertheless, functional heterogeneity has been found between the two homologues. Here we report the solution structure of SUMO-3 C47S (residues 14-92) featuring the beta-beta-alpha-beta-beta-alpha-beta ubiquitin fold. Structural comparison shows that SUMO-3 C47S resembles ubiquitin more than SUMO-1. On the helix-sheet interface, a strong hydrophobic interaction contributes to formation of the globular and compact fold. A Gly-Gly motif at the C-terminal tail, extending away from the core structure, is accessible to enzymes and substrates. In vivo, SUMO modification proceeds via a multistep pathway, and Ubc9 plays an indispensable role as the SUMO conjugating enzyme (E2) in this process. To develop a better understanding of SUMO-3 conjugation, the Ubc9 binding surface on SUMO-3 C47S has been detected by chemical shift perturbation using NMR spectroscopy. The binding site mainly resides on the hydrophilic side of the beta-sheet. Negatively charged and hydrophobic residues of this region are highly or moderately conserved among SUMO family members. Notably, the negatively charged surface of SUMO-3 C47S is highly complementary in its electrostatic potentials and hydrophobicity to the positively charged surface of Ubc9. This work indicates dissimilarities between SUMO-3 and SUMO-1 in tertiary structure and provides insight into the specific interactions of SUMO-3 with its modifying enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2790-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15723523-Amino Acid Sequence, pubmed-meshheading:15723523-Amino Acid Substitution, pubmed-meshheading:15723523-Binding Sites, pubmed-meshheading:15723523-Humans, pubmed-meshheading:15723523-Magnetic Resonance Spectroscopy, pubmed-meshheading:15723523-Models, Molecular, pubmed-meshheading:15723523-Molecular Sequence Data, pubmed-meshheading:15723523-Mutagenesis, Site-Directed, pubmed-meshheading:15723523-Protein Conformation, pubmed-meshheading:15723523-Protein Structure, Tertiary, pubmed-meshheading:15723523-Sequence Alignment, pubmed-meshheading:15723523-Sequence Homology, Amino Acid, pubmed-meshheading:15723523-Small Ubiquitin-Related Modifier Proteins, pubmed-meshheading:15723523-Solutions, pubmed-meshheading:15723523-Ubiquitin, pubmed-meshheading:15723523-Ubiquitin-Conjugating Enzymes
pubmed:year
2005
pubmed:articleTitle
Solution structure of human SUMO-3 C47S and its binding surface for Ubc9.
pubmed:affiliation
School of Life Sciences, University of Science and Technology of China, and Hefei National Laboratory for Physical Sciences at Microscale, Hefei, Anhui 230026, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't