This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1qqe

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 11:21, 4 December 2019

CRYSTAL STRUCTURE OF THE VESICULAR TRANSPORT PROTEIN SEC17

Structural highlights

1qqe is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SEC17_YEAST] SNARE complex protein that binds to cis-SNARE complexes on membranes and is required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus and for homotypic vacuole fusion. During the priming step of membrane fusion, is released from cis-SNARE complexes by SEC18 to establish a pool of unpaired SNAREs, which are required for interactions in trans during docking and fusion steps. Can displace HOPS from SNARE complexes, which may be a prerequisite for trans-SNARE complex disassembly and subsequent rounds of priming, docking and fusion.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly.,Rice LM, Brunger AT Mol Cell. 1999 Jul;4(1):85-95. PMID:10445030^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mayer A, Wickner W, Haas A. Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell. 1996 Apr 5;85(1):83-94. PMID:8620540
↑ Haas A, Wickner W. Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF). EMBO J. 1996 Jul 1;15(13):3296-305. PMID:8670830
↑ Nichols BJ, Ungermann C, Pelham HR, Wickner WT, Haas A. Homotypic vacuolar fusion mediated by t- and v-SNAREs. Nature. 1997 May 8;387(6629):199-202. PMID:9144293 doi:http://dx.doi.org/10.1038/387199a0
↑ Collins KM, Thorngren NL, Fratti RA, Wickner WT. Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion. EMBO J. 2005 May 18;24(10):1775-86. Epub 2005 May 5. PMID:15889152 doi:http://dx.doi.org/7600658
↑ Rice LM, Brunger AT. Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly. Mol Cell. 1999 Jul;4(1):85-95. PMID:10445030

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qqe"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF THE VESICULAR TRANSPORT PROTEIN SEC17==
-<StructureSection load='1qqe' size='340' side='right' caption='[[1qqe]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='1qqe' size='340' side='right'caption='[[1qqe]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1qqe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QQE FirstGlance]. <br>
@@ Line 32: / Line 32: @@
 </StructureSection>
 [[Category: Atcc 18824]]
+[[Category: Large Structures]]
 [[Category: Brunger, A T]]
 [[Category: Rice, L M]]
 [[Category: Helix-turn-helix tpr-like repeat]]
 [[Category: Protein transport]]

1qqe

From Proteopedia

Revision as of 11:21, 4 December 2019

CRYSTAL STRUCTURE OF THE VESICULAR TRANSPORT PROTEIN SEC17

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox