1kmk: Difference between revisions

Revision as of 10:33, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kmk.png

Template:STRUCTURE 1kmk

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).

Template:ABSTRACT PUBMED 11853669

About this StructureAbout this Structure

1KMK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Wed Jul 2 10:33:39 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''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).===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11853669}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11853669 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11853669}}
 ==About this Structure==
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 [[Category: Psi]]
 [[Category: Structural genomic]]
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