2W3C

Globular head region of the human general vesicular transport factor p115

Summary for 2W3C

• Entry DOI: 10.2210/pdb2w3c/pdb
• Descriptor: GENERAL VESICULAR TRANSPORT FACTOR P115, DI(HYDROXYETHYL)ETHER (3 entities in total)
• Functional Keywords: membrane vesicle tethering, armadillo fold, golgi apparatus, er-golgi transport, endoplasmatic reticulum, p115, golgi, uso1p, golgin, membrane, transport protein
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm, cytosol: O60763
• Total number of polymer chains: 1
• Total formula weight: 64660.90

Authors

Striegl, H.,Roske, Y.,Kummel, D.,Heinemann, U. (deposition date: 2008-11-11, release date: 2009-03-03, Last modification date: 2024-05-08)

Primary citation

Striegl, H.,Roske, Y.,Kummel, D.,Heinemann, U.
Unusual Armadillo Fold in the Human General Vesicular Transport Factor P115
Plos One, 4:E4656-, 2009

PubMed Abstract: The golgin family gives identity and structure to the Golgi apparatus and is part of a complex protein network at the Golgi membrane. The golgin p115 is targeted by the GTPase Rab1a, contains a large globular head region and a long region of coiled-coil which forms an extended rod-like structure. p115 serves as vesicle tethering factor and plays an important role at different steps of vesicular transport. Here we present the 2.2 A-resolution X-ray structure of the globular head region of p115. The structure exhibits an armadillo fold that is decorated by elongated loops and carries a C-terminal non-canonical repeat. This terminal repeat folds into the armadillo superhelical groove and allows homodimeric association with important implications for p115 mediated multiple protein interactions and tethering.

PubMed: 19247479
DOI: 10.1371/JOURNAL.PONE.0004656

Experimental method

X-RAY DIFFRACTION (2.22 Å)