3E73

Crystal Structure of Human LanCL1 complexed with GSH

Summary for 3E73

• Entry DOI: 10.2210/pdb3e73/pdb
• Related: 3E6U
• Descriptor: LanC-like protein 1, ZINC ION, GLUTATHIONE, ... (4 entities in total)
• Functional Keywords: alpha helix barrel, cytoplasm, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: O43813
• Total number of polymer chains: 2
• Total formula weight: 94514.71

Authors

Zhang, W.,Zhu, G.,Li, X.,Rao, Z.,Zhang, C. (deposition date: 2008-08-17, release date: 2009-06-30, Last modification date: 2023-11-01)

Primary citation

Zhang, W.,Wang, L.,Liu, Y.,Xu, J.,Zhu, G.,Cang, H.,Li, X.,Bartlam, M.,Hensley, K.,Li, G.,Rao, Z.,Zhang, X.C.
Structure of human lanthionine synthetase C-like protein 1 and its interaction with Eps8 and glutathione
Genes Dev., 23:1387-1392, 2009

PubMed Abstract: Eukaryotic lanthionine synthetase C-like protein 1 (LanCL1) is homologous to prokaryotic lanthionine cyclases, yet its biochemical functions remain elusive. We report the crystal structures of human LanCL1, both free of and complexed with glutathione, revealing glutathione binding to a zinc ion at the putative active site formed by conserved GxxG motifs. We also demonstrate by in vitro affinity analysis that LanCL1 binds specifically to the SH3 domain of a signaling protein, Eps8. Importantly, expression of LanCL1 mutants defective in Eps8 interaction inhibits nerve growth factor (NGF)-induced neurite outgrowth, providing evidence for the biological significance of this novel interaction in cellular signaling and differentiation.

PubMed: 19528316
DOI: 10.1101/gad.1789209

Experimental method

X-RAY DIFFRACTION (2.8 Å)