PDBsum entry 2w3c

Transport protein

PDB id

2w3c

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Contents

			Protein chain

					551 a.a. *

			Ligands

					PEG ×3

			Waters ×123

* Residue conservation analysis

PDB id:

2w3c

Links

Name:

Transport protein

Title:

Globular head region of the human general vesicular transport factor p115

Structure:

General vesicular transport factor p115. Chain: a. Fragment: armadillo helical domain, uso1 head domain, residues 53- 629. Synonym: protein uso1 homolog, transcytosis-associated protein, vesicle-docking protein. Engineered: yes. Other_details: lacking n-terminal residues 1-53 and putativE C- terminal coiled-coil domain (630-962)

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.22Å

R-factor:

0.222

R-free:

0.269

Authors:

H.Striegl,Y.Roske,D.Kummel,U.Heinemann

Key ref:

H.Striegl et al. (2009). Unusual armadillo fold in the human general vesicular transport factor p115. Plos One, 4, e4656. PubMed id: 19247479

Date:

11-Nov-08

Release date:

03-Mar-09

PROCHECK

	Headers

	References

Protein chain

O60763 (USO1_HUMAN) - General vesicular transport factor p115 from Homo sapiens

Seq: Struc:

Seq: Struc:					962 a.a. 551 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

	Plos One 4:e4656 (2009)
PubMed id: 19247479

Unusual armadillo fold in the human general vesicular transport factor p115.
H.Striegl, Y.Roske, D.Kümmel, U.Heinemann.

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.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20130678

C.A.Ewens, P.Kloppsteck, A.Förster, X.Zhang, and P.S.Freemont (2010).
Structural and functional implications of phosphorylation and acetylation in the regulation of the AAA+ protein p97.

Biochem Cell Biol, 88, 41-48.

20126549

H.Striegl, M.A.Andrade-Navarro, and U.Heinemann (2010).
Armadillo motifs involved in vesicular transport.

PLoS One, 5, e8991.

19887069

E.Sztul, and V.Lupashin (2009).
Role of vesicle tethering factors in the ER-Golgi membrane traffic.

FEBS Lett, 583, 3770-3783.

19777061

F.Kippert, and D.L.Gerloff (2009).
Highly sensitive detection of individual HEAT and ARM repeats with HHpred and COACH.

PLoS One, 4, e7148.

19835610

J.Guergnon, U.Derewenda, J.R.Edelson, and D.L.Brautigan (2009).
Mapping of protein phosphatase-6 association with its SAPS domain regulatory subunit using a model of helical repeats.

BMC Biochem, 10, 24.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.