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2px9

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2px9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2px9 OCA], [http://www.ebi.ac.uk/pdbsum/2px9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2px9 RCSB]</span>
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[[Category: ubiquitination]]
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Revision as of 01:41, 31 March 2008

Image:2px9.gif


PDB ID 2px9

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



The intrinsic affinity between E2 and the Cys domain of E1 in Ubiquitin-like modifications


Overview

Ubiquitin-like modifications, which are carried out by similar biochemical mechanisms, regulate nearly every aspect of cellular function. Despite the recent advancements in characterizing their enzymology, our knowledge about the dynamic processes of these modifications is still fragmentary. In this study, we have uncovered an intrinsic affinity between the SUMO E2 and the Cys domain of SUMO E1. NMR studies in combination with paramagnetic spin labeling demonstrate that this interaction is mediated by previously unknown interfaces on both E1 and E2 and places the two catalytic Cys residues of the two enzymes in close proximity. Site-directed mutagenesis and enzymatic assays indicate that the interaction is fundamentally important for the transfer of SUMO from E1 to E2. Results from this study suggest that the interaction between E2 and the Cys domain of E1 participates in guiding the E2's translocation to E1's enzymatic active site in ubiquitin-like modifications.

About this Structure

2PX9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications., Wang J, Hu W, Cai S, Lee B, Song J, Chen Y, Mol Cell. 2007 Jul 20;27(2):228-37. PMID:17643372

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