1kmk
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1kmk.gif|left|200px]] | [[Image:1kmk.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1kmk", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1kmk| PDB=1kmk | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).''' | '''E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).''' | ||
| Line 29: | Line 26: | ||
[[Category: Lima, C D.]] | [[Category: Lima, C D.]] | ||
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | ||
| - | [[Category: | + | [[Category: New york structural genomix research consortium]] |
| - | [[Category: | + | [[Category: Nifs selenocysteine cysteine persulfide perselenide xray]] |
| - | [[Category: | + | [[Category: Nysgxrc]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:55:07 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:55, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 22:55:07 2008
Categories: Escherichia coli | Selenocysteine lyase | Single protein | Burley, S K. | Lima, C D. | NYSGXRC, New York Structural GenomiX Research Consortium. | New york structural genomix research consortium | Nifs selenocysteine cysteine persulfide perselenide xray | Nysgxrc | Protein structure initiative | Psi | Structural genomic
