1kmj: Difference between revisions

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Revision as of 06:55, 26 March 2008

File:1kmj.gif

, resolution 2.0Å

Ligands:

,

Activity:

Selenocysteine lyase, with EC number 4.4.1.16

Domains:

PRK09295, csdA

Resources:

FirstGlance, OCA, PDBsum, JenaLib, RCSB

Coordinates:

save as pdb, mmCIF, xml

E. coli NifS/CsdB protein at 2.0A with the cysteine persulfide intermediate (residue CSS).

OverviewOverview

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 StructureAbout this Structure

1KMJ 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 Mar 26 05:55:06 2008

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

OCA

@@ Line 4: / Line 4: @@
 |PDB= 1kmj |SIZE=350|CAPTION= <scene name='initialview01'>1kmj</scene>, resolution 2.0&Aring;
 |SITE=
-|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
+|LIGAND= <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Selenocysteine_lyase Selenocysteine lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.16 4.4.1.16]
+|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Selenocysteine_lyase Selenocysteine lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.16 4.4.1.16] </span>
 |GENE=
+|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK09295 PRK09295], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0520 csdA]</span>
+|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmj OCA], [http://www.ebi.ac.uk/pdbsum/1kmj PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1kmj RCSB]</span>
 }}
@@ Line 26: / Line 28: @@
 [[Category: Lima, C D.]]
 [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
-[[Category: PLP]]
 [[Category: new york structural genomix research consortium]]
 [[Category: nysgxrc]]
@@ Line 34: / Line 35: @@
 [[Category: structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:30:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:55:06 2008''