2esp

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[[Image:2esp.gif|left|200px]]<br /><applet load="2esp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2esp.gif|left|200px]]
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caption="2esp, resolution 1.52&Aring;" />
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'''Human ubiquitin-conjugating enzyme (E2) UbcH5b mutant Ile88Ala'''<br />
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{{Structure
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|PDB= 2esp |SIZE=350|CAPTION= <scene name='initialview01'>2esp</scene>, resolution 1.52&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19]
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|GENE= UBE2D2, UBC4, UBCH5B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Human ubiquitin-conjugating enzyme (E2) UbcH5b mutant Ile88Ala'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2ESP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESP OCA].
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2ESP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESP OCA].
==Reference==
==Reference==
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Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases., Ozkan E, Yu H, Deisenhofer J, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18890-5. Epub 2005 Dec 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16365295 16365295]
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Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases., Ozkan E, Yu H, Deisenhofer J, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18890-5. Epub 2005 Dec 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16365295 16365295]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: ligase]]
[[Category: ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:43:55 2008''

Revision as of 14:43, 20 March 2008

Image:2esp.gif


PDB ID 2esp

Drag the structure with the mouse to rotate
, resolution 1.52Å
Ligands: and
Gene: UBE2D2, UBC4, UBCH5B (Homo sapiens)
Activity: Ubiquitin--protein ligase, with EC number 6.3.2.19
Coordinates: save as pdb, mmCIF, xml



Human ubiquitin-conjugating enzyme (E2) UbcH5b mutant Ile88Ala


Overview

Ubiquitin-conjugating enzymes (E2s) collaborate with the ubiquitin-activating enzyme (E1) and ubiquitin ligases (E3s) to attach ubiquitin to target proteins. RING-containing E3s simultaneously bind to E2s and substrates, bringing them into close proximity and thus facilitating ubiquitination. We show herein that, although the E3-binding site on the human E2 UbcH5b is distant from its active site, two RING-type minimal E3 modules lacking substrate-binding functions greatly stimulate the rate of ubiquitin release from the UbcH5b-ubiquitin thioester. Using statistical coupling analysis and mutagenesis, we identify and characterize clusters of coevolving and functionally linked residues within UbcH5b that span its E3-binding and active sites. Several UbcH5b mutants are defective in their stimulation by E3s despite their abilities to bind to these E3s, to form ubiquitin thioesters, and to release ubiquitin at a basal rate. One such mutation, I37A, is distant from both the active site and the E3-binding site of UbcH5b. Our studies reveal structural determinants for communication between distal functional sites of E2s and suggest that RING-type E3s activate E2s allosterically.

About this Structure

2ESP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases., Ozkan E, Yu H, Deisenhofer J, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18890-5. Epub 2005 Dec 19. PMID:16365295

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