This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1a5r

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /><applet load="1a5r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a5r" /> '''STRUCTURE DETERMINATION OF THE SMALL UBIQUIT...)
Next diff →

Revision as of 08:30, 20 November 2007


1a5r

Drag the structure with the mouse to rotate

STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN-RELATED MODIFIER SUMO-1, NMR, 10 STRUCTURES

Overview

The recently discovered small ubiquitin-related modifier SUMO-1 belongs to, the growing family of ubiquitin-related proteins involved in, postranslational protein modification. Unlike ubiquitin, SUMO-1 does not, appear to target proteins for degradation but seems to be involved in the, modulation of protein-protein interactions. Independent studies, demonstrate an essential function of SUMO-1 in the regulation of, nucleo-cytoplasmic transport, and suggest a role in cell-cycle regulation, and apoptosis. Here, we present the first three-dimensional structure of, SUMO-1 solved by NMR. Although having only 18% amino acid sequence, identity with ubiquitin, the overall structure closely resembles that of, ubiquitin, featuring the betabetaalphabetabetaalphabeta fold of the, ubiquitin protein family. In addition, the position of the two C-terminal, Gly residues required for isopeptide bond formation is conserved between, ubiquitin and SUMO-1. The most prominent feature of SUMO-1 is a long and, highly flexible N terminus, which protrudes from the core of the protein, and which is absent in ubiquitin. Furthermore, ubiquitin Lys48, required, to generate ubiquitin polymers, is substituted in SUMO-1 by Gln69 at the, same position, which provides an explanation of why SUMO-1 has not been, observed to form polymers. Moreover, the hydrophobic core of SUMO-1 and, ubiquitin is maintained by conserved hydrophobic residues, whereas the, overall charge topology of SUMO-1 and ubiquitin differs significantly, suggesting specific modifying enzymes and target proteins for both, proteins.

About this Structure

1A5R is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure determination of the small ubiquitin-related modifier SUMO-1., Bayer P, Arndt A, Metzger S, Mahajan R, Melchior F, Jaenicke R, Becker J, J Mol Biol. 1998 Jul 10;280(2):275-86. PMID:9654451

Page seeded by OCA on Tue Nov 20 10:37:43 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools