PDBsum entry 1qqe

Protein transport

PDB id: 1qqe

Contents

Protein chain

281 a.a. *

Waters ×4

* Residue conservation analysis

PDB id:

1qqe

Name:

Protein transport

Title:

Crystal structure of the vesicular transport protein sec17

Structure:

Vesicular transport protein sec17. Chain: a. Engineered: yes. Mutation: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.90Å R-factor: 0.260 R-free: 0.283

Authors:

L.M.Rice,A.T.Brunger

Key ref:

L.M.Rice and A.T.Brunger (1999). Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly. Mol Cell, 4, 85-95. PubMed id: 10445030 DOI: 10.1016/S1097-2765(00)80190-2

Date:

04-Jun-99 Release date: 08-Sep-99

Protein chain

P32602  (SEC17_YEAST) -  Alpha-soluble NSF attachment protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 292 a.a.

Struc: 281 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/S1097-2765(00)80190-2

Mol Cell 4:85-95 (1999)

PubMed id: 10445030

Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly.

L.M.Rice, A.T.Brunger.

ABSTRACT

SNAP proteins play an essential role in membrane trafficking in eukaryotic cells. They activate and recycle SNARE proteins by serving as adaptors between SNAREs and the cytosolic chaperone NSF. We have determined the crystal structure of Sec17, the yeast homolog of alpha-SNAP, to 2.9 A resolution. Sec17 is composed of an N-terminal twisted sheet of alpha-helical hairpins and a C-terminal alpha-helical bundle. The N-terminal sheet has local similarity to the tetratricopeptide repeats from protein phosphatase 5 but has a different overall twist. Sec17 also shares structural features with HEAT and clathrin heavy chain repeats. Possible models of SNAP:SNARE binding suggest that SNAPs may function as lever arms, transmitting forces generated by conformational changes in NSF/Sec18 to drive disassembly of SNARE complexes.

Selected figure(s)

Figure 1.
Figure 1. Experimental Electron Density Map after Density ModificationDensity-modified experimental electron density for α helices α3 and α4 and the connecting loop contoured at 1.4 σ. The final, refined model is shown using a ball-and-stick representation. The α helices, loop, and most side chains are clearly visible in the initial map. The buried residues Gly-57, Phe-60, Ala-83, and Phe-87, which are conserved in the representative SNAP sequences (Figure 3A), are depicted in red.

Figure 2.
Figure 2. Overall Structure of Sec17Two ribbon drawings of Sec17 related by a 180° rotation around the long axis of the protein. The nine N-terminal α helices form a twisted sheet that gives rise to two faces and two ridges. The five C-terminal α helices form a more globular bundle, which is asymmetrically disposed with respect to the N-terminal sheet, creating a significant cleft on one face of the molecule. Residues colored red and yellow correspond, respectively, to inhibitory and noninhibitory peptides from an earlier study ([15]).

The above figures are reprinted by permission from Cell Press: Mol Cell (1999, 4, 85-95) copyright 1999.

Figures were selected by an automated process.