1kmk

From Proteopedia

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Revision as of 17:15, 20 November 2007

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spinqualitylabelsall models 1kmk, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).

Overview

E2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to, lysine residues directly or through E3-mediated reactions. The small, ubiquitin-like modifier SUMO regulates nuclear transport, stress response, and signal transduction in eukaryotes and is essential for cell-cycle, progression in yeast. In contrast to most ubiquitin conjugation, the SUMO, E2 enzyme Ubc9 is sufficient for substrate recognition and lysine, modification of known SUMO targets. Crystallographic analysis of a complex, between mammalian Ubc9 and a C-terminal domain of RanGAP1 at 2.5 A reveals, structural determinants for recognition of consensus SUMO modification, sequences found within SUMO-conjugated proteins. Structure-based, mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct, motifs required for substrate binding and SUMO modification of p53, IkappaBalpha, and RanGAP1.

About this Structure

1KMK is a Single protein structure of sequence from Escherichia coli with CSE and PLP as ligands. Active as Selenocysteine lyase, with EC number 4.4.1.16 Full crystallographic information is available from OCA.

Reference

Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1., Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD, Cell. 2002 Feb 8;108(3):345-56. PMID:11853669

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