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.


1cr5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cr5.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1cr5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cr5| PDB=1cr5 | SCENE= }}
{{STRUCTURE_1cr5| PDB=1cr5 | SCENE= }}
-
'''N-TERMINAL DOMAIN OF SEC18P'''
+
===N-TERMINAL DOMAIN OF SEC18P===
-
==Overview==
+
<!--
-
Yeast Sec18p and its mammalian orthologue N-ethylmaleimide-sensitive fusion protein (NSF) are hexameric ATPases with a central role in vesicle trafficking. Aided by soluble adapter factors (SNAPs), Sec18p/NSF induces ATP-dependent disassembly of a complex of integral membrane proteins from the vesicle and target membranes (SNAP receptors). During the ATP hydrolysis cycle, the Sec18p/NSF homohexamer undergoes a large-scale conformational change involving repositioning of the most N terminal of the three domains of each protomer, a domain that is required for SNAP-mediated interaction with SNAP receptors. Whether an internal conformational change in the N-terminal domains accompanies their reorientation with respect to the rest of the hexamer remains to be addressed. We have determined the structure of the N-terminal domain from Sec18p by x-ray crystallography. The Sec18p N-terminal domain consists of two beta-sheet-rich subdomains connected by a short linker. A conserved basic cleft opposite the linker may constitute a SNAP-binding site. Despite structural variability in the linker region and in an adjacent loop, all three independent molecules in the crystal asymmetric unit have the identical subdomain interface, supporting the notion that this interface is a preferred packing arrangement. However, the linker flexibility allows for the possibility that other subdomain orientations may be sampled.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10611286}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10611286 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10611286}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Double-psi beta barrel]]
[[Category: Double-psi beta barrel]]
[[Category: Vesicle fusion]]
[[Category: Vesicle fusion]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:01:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:11:52 2008''

Revision as of 18:11, 30 June 2008

Image:1cr5.png

Template:STRUCTURE 1cr5

N-TERMINAL DOMAIN OF SEC18P

Template:ABSTRACT PUBMED 10611286

About this Structure

1CR5 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Sec18p N-terminal domain., Babor SM, Fass D, Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14759-64. PMID:10611286

Page seeded by OCA on Mon Jun 30 21:11:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cr5"
Personal tools