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4bwf

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{{STRUCTURE_4bwf| PDB=4bwf | SCENE= }}
{{STRUCTURE_4bwf| PDB=4bwf | SCENE= }}
===Pex4p-Pex22p disulphide bond mutant===
===Pex4p-Pex22p disulphide bond mutant===
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{{ABSTRACT_PUBMED_23896733}}
==Function==
==Function==
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==About this Structure==
==About this Structure==
[[4bwf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2y9o 2y9o]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWF OCA].
[[4bwf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2y9o 2y9o]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWF OCA].
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==Reference==
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<ref group="xtra">PMID:023896733</ref><references group="xtra"/><references/>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Ubiquitin--protein ligase]]

Revision as of 18:56, 7 August 2013

Template:STRUCTURE 4bwf

Contents

Pex4p-Pex22p disulphide bond mutant

Template:ABSTRACT PUBMED 23896733

Function

[UBCX_YEAST] Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis. Required for UBC4-independent ubiquitination of PEX5. [PEX22_YEAST] Involved in peroxisome biogenesis (By similarity).

About this Structure

4bwf is a 2 chain structure with sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entry 2y9o. Full crystallographic information is available from OCA.

Reference

  • Williams C, van den Berg M, Stanley WA, Wilmanns M, Distel B. A disulphide bond in the E2 enzyme Pex4p modulates ubiquitin-conjugating activity. Sci Rep. 2013 Jul 30;3:2212. doi: 10.1038/srep02212. PMID:23896733 doi:10.1038/srep02212

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