PDBsum entry 4q66

Protein transport

PDB id: 4q66

Contents

Protein chains

226 a.a.

158 a.a.

211 a.a.

171 a.a.

593 a.a.

557 a.a.

507 a.a.

338 a.a.

146 a.a.

139 a.a.

134 a.a.

86 a.a.

Ligands

GNP ×4

Metals

_MG ×4

PDB id:

4q66

Name:

Protein transport

Title:

Structure of exomer bound to arf1.

Structure:

Chs5p. Chain: a, j, g, d. Synonym: protein cal3. Engineered: yes. Protein bch1. Chain: k, e, b, h. Synonym: bud7 and chs6 homolog 1. Engineered: yes. Adp-ribosylation factor 1.

Source:

Saccharomyces cerevisiae r008. Baker's yeast. Organism_taxid: 1182966. Strain: atcc 204508 / s288c. Gene: cal3, chs5, l8543.18, r008_l12446, ylr330w. Expressed in: escherichia coli. Expression_system_taxid: 562. Saccharomyces cerevisiae. Organism_taxid: 559292.

Resolution:

3.35Å R-factor: 0.280 R-free: 0.310

Authors:

J.E.Paczkowski,J.C.Fromme

Key ref:

J.E.Paczkowski and J.C.Fromme (2014). Structural basis for membrane binding and remodeling by the exomer secretory vesicle cargo adaptor. Dev Cell, 30, 610-624. PubMed id: 25203211 DOI: 10.1016/j.devcel.2014.07.014

Date:

21-Apr-14 Release date: 17-Sep-14

Protein chain

No UniProt id for this chain

Struc: 226 a.a.

Protein chain

No UniProt id for this chain

Struc: 158 a.a.

Protein chain

No UniProt id for this chain

Struc: 211 a.a.

Protein chain

No UniProt id for this chain

Struc: 171 a.a.

Protein chain

Q05029  (BCH1_YEAST) -  Protein BCH1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 724 a.a.

Struc: 593 a.a.

Protein chain

Q05029  (BCH1_YEAST) -  Protein BCH1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 724 a.a.

Struc: 557 a.a.

Protein chain

Q05029  (BCH1_YEAST) -  Protein BCH1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 724 a.a.

Struc: 507 a.a.*

Protein chain

Q05029  (BCH1_YEAST) -  Protein BCH1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 724 a.a.

Struc: 338 a.a.*

Protein chain

P11076  (ARF1_YEAST) -  ADP-ribosylation factor 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 181 a.a.

Struc: 146 a.a.*

Protein chain

P11076  (ARF1_YEAST) -  ADP-ribosylation factor 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 181 a.a.

Struc: 139 a.a.*

Protein chain

P11076  (ARF1_YEAST) -  ADP-ribosylation factor 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 181 a.a.

Struc: 134 a.a.*

Protein chain

P11076  (ARF1_YEAST) -  ADP-ribosylation factor 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 181 a.a.

Struc: 86 a.a.*

* PDB and UniProt seqs differ at 33 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chains K, E, B, H: E.C.?
• Enzyme class 3: Chains F, L, C, I: E.C.3.6.5.2 - small monomeric GTPase.
• Reaction: GTP + H2O = GDP + phosphate + H⁺

GTP + H2O = GDP (Bound ligand (Het Group name = GNP) matches with 81.82% similarity) + phosphate + H(+)

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.devcel.2014.07.014

Dev Cell 30:610-624 (2014)

PubMed id: 25203211

Structural basis for membrane binding and remodeling by the exomer secretory vesicle cargo adaptor.

J.E.Paczkowski, J.C.Fromme.

ABSTRACT

Cargo adaptor subunits of vesicle coat protein complexes sort transmembrane proteins to distinct membrane compartments in eukaryotic cells. The exomer complex is the only cargo adaptor known to sort proteins at the trans-Golgi network into secretory vesicles. Exomer function is regulated by the Arf1 GTPase, a master regulator of trafficking at the Golgi. We report the structure of exomer bound to two copies of Arf1. Exomer interacts with each Arf1 molecule via two surfaces, one of which is a noncanonical interface that regulates GTP hydrolysis. The structure uncovers an unexpected membrane-proximal hydrophobic element that exomer uses in cooperation with Arf1 to remodel membranes. Given the constrained motion of the exomer hinge region, we envision that exomer dynamically positions multiple membrane insertion elements to drive membrane fission. In contrast to other known cargo adaptors, exomer therefore couples two functions, cargo sorting and membrane fission, into a single complex.