3GBW

Crystal structure of the first PHR domain of the Mouse Myc-binding protein 2 (MYCBP-2)

Summary for 3GBW

• Entry DOI: 10.2210/pdb3gbw/pdb
• Descriptor: E3 ubiquitin-protein ligase MYCBP2 (2 entities in total)
• Functional Keywords: myc-binding protein 2, mycbp2, probable e3 ubiquitin-protein ligase mycbp2, protein associated with myc, pam, rpm-1, phr domain, structural genomics, psi-2, protein structure initiative, new york structural genomix research consortium, nysgxrc, alternative splicing, ligase, metal-binding, nucleus, phosphoprotein, transcription, transcription regulation, ubl conjugation pathway, zinc, zinc-finger, new york sgx research center for structural genomics
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 1
• Total formula weight: 17816.22

Authors

Sampathkumar, P.,Ozyurt, S.A.,Wasserman, S.R.,Klemke, R.L.,Miller, S.A.,Bain, K.T.,Rutter, M.E.,Tarun, G.,Atwell, S.,Sauder, J.M.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2009-02-20, release date: 2009-03-24, Last modification date: 2024-10-30)

Primary citation

Sampathkumar, P.,Ozyurt, S.A.,Miller, S.A.,Bain, K.T.,Rutter, M.E.,Gheyi, T.,Abrams, B.,Wang, Y.,Atwell, S.,Luz, J.G.,Thompson, D.A.,Wasserman, S.R.,Emtage, J.S.,Park, E.C.,Rongo, C.,Jin, Y.,Klemke, R.L.,Sauder, J.M.,Burley, S.K.
Structures of PHR domains from Mus musculus Phr1 (Mycbp2) explain the loss-of-function mutation (Gly1092-->Glu) of the C. elegans ortholog RPM-1.
J.Mol.Biol., 397:883-892, 2010

PubMed Abstract: PHR [PAM (protein associated with Myc)-HIW (Highwire)-RPM-1 (regulator of presynaptic morphology 1)] proteins are conserved, large multi-domain E3 ubiquitin ligases with modular architecture. PHR proteins presynaptically control synaptic growth and axon guidance and postsynaptically regulate endocytosis of glutamate receptors. Dysfunction of neuronal ubiquitin-mediated proteasomal degradation is implicated in various neurodegenerative diseases. PHR proteins are characterized by the presence of two PHR domains near the N-terminus, which are essential for proper localization and function. Structures of both the first and second PHR domains of Mus musculus (mouse) Phr1 (MYC binding protein 2, Mycbp2) have been determined, revealing a novel beta sandwich fold composed of 11 antiparallel beta-strands. Conserved loops decorate the apical side of the first PHR domain (MmPHR1), yielding a distinct conserved surface feature. The surface of the second PHR domain (MmPHR2), in contrast, lacks significant conservation. Importantly, the structure of MmPHR1 provides insights into a loss-of-function mutation, Gly1092-->Glu, observed in the Caenorhabditis elegans ortholog RPM-1.

PubMed: 20156452
DOI: 10.1016/j.jmb.2010.02.017

Experimental method

X-RAY DIFFRACTION (1.32 Å)