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1kmk

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[[Image:1kmk.gif|left|200px]]<br /><applet load="1kmk" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kmk.gif|left|200px]]
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caption="1kmk, resolution 2.2&Aring;" />
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'''E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).'''<br />
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{{Structure
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|PDB= 1kmk |SIZE=350|CAPTION= <scene name='initialview01'>1kmk</scene>, resolution 2.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CSE:SELENOCYSTEINE'>CSE</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>
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|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]
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|GENE=
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}}
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'''E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1KMK 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=CSE:'>CSE</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1KMK OCA].
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1KMK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMK OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11853669 11853669]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11853669 11853669]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Selenocysteine lyase]]
[[Category: Selenocysteine lyase]]
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[[Category: protein structure initiative]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:25 2008''

Revision as of 10:19, 20 March 2008

Image:1kmk.gif


PDB ID 1kmk

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: and
Activity: Selenocysteine lyase, with EC number 4.4.1.16
Coordinates: save as pdb, mmCIF, xml



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 Thu Mar 20 12:19:25 2008

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