1kmk: Difference between revisions
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New page: left|200px<br /><applet load="1kmk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kmk, resolution 2.2Å" /> '''E. coli NifS/CsdB pro... |
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[[Image:1kmk.gif|left|200px]]<br /><applet load="1kmk" size=" | [[Image:1kmk.gif|left|200px]]<br /><applet load="1kmk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1kmk, resolution 2.2Å" /> | caption="1kmk, resolution 2.2Å" /> | ||
'''E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).'''<br /> | '''E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).'''<br /> | ||
==Overview== | ==Overview== | ||
E2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to | 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== | ==About this Structure== | ||
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 CSE and PLP 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:// | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Selenocysteine lyase]] | [[Category: Selenocysteine lyase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Burley, S | [[Category: Burley, S K.]] | ||
[[Category: Lima, C | [[Category: Lima, C D.]] | ||
[[Category: NYSGXRC, New | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] | ||
[[Category: CSE]] | [[Category: CSE]] | ||
[[Category: PLP]] | [[Category: PLP]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:43 2008'' | ||
