1kmj: Difference between revisions

Revision as of 14:35, 21 February 2008

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 with as ligand. Active as Selenocysteine lyase, with EC number 4.4.1.16 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 Thu Feb 21 13:35:44 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:1kmj.gif|left|200px]]<br /><applet load="1kmj" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1kmj.gif|left|200px]]<br /><applet load="1kmj" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1kmj, resolution 2.0&Aring;" />
 '''E. coli NifS/CsdB protein at 2.0A with the cysteine persulfide intermediate (residue CSS).'''<br />
 ==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.
+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==
-KMJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KMJ OCA].
+KMJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMJ OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Selenocysteine lyase]]
 [[Category: Single protein]]
-[[Category: Burley, S.K.]]
+[[Category: Burley, S K.]]
-[[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: PLP]]
 [[Category: new york structural genomix research consortium]]
@@ Line 25: / Line 25: @@
 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:22:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:44 2008''