First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.

1vzj

From Proteopedia

Jump to: navigation, search


1vzj, resolution 2.35Å ()
Non-Standard Residues:
Activity: Acetylcholinesterase, with EC number 3.1.1.7
Related: 1b41, 1f8u, 2clj
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT-HANDED POLYPROLINE HELIX

Contents

Overview

Functional localization of acetylcholinesterase (AChE) in vertebrate muscle and brain depends on interaction of the tryptophan amphiphilic tetramerization sequence at the C-terminus of its major splice variant (T) with a proline-rich attachment domain of the anchoring proteins collagenous (ColQ) and proline-rich membrane anchor. The crystal structure of the reveals a novel supercoil structure in which four parallel WAT chains form a left-handed superhelix around an antiparallel left-handed PRAD helix resembling polyproline II. The WAT coiled coils possess a WWW motif making repetitive hydrophobic stacking and hydrogen-bond interactions with the PRAD. The WAT chains are related by an approximately 4-fold screw axis around the PRAD. Each WAT makes similar but unique interactions consistent with an asymmetric pattern of disulfide linkages between the AChE tetramer subunits and ColQ. The P59Q mutation in ColQ, which causes congenital endplate AChE deficiency and is located within the PRAD, disrupts crucial WAT-WAT and WAT-PRAD interactions. (model coordinates)

Disease

Known diseases associated with this structure: Blood group, Yt system OMIM:[100740], Endplate acetylcholinesterase deficiency OMIM:[603033]

About this Structure

1VZJ is a Protein complex structure of sequences from Homo sapiens. Active as Acetylcholinesterase, with EC number 3.1.1.7 Full crystallographic information is available from OCA.

Reference

The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix., Dvir H, Harel M, Bon S, Liu WQ, Vidal M, Garbay C, Sussman JL, Massoulie J, Silman I, EMBO J. 2004 Nov 10;23(22):4394-405. Epub 2004 Nov 4. PMID:15526038

Page seeded by OCA on Mon Nov 12 19:45:11 2007

Proteopedia Page Contributors and Editors (what is this?)

Eran Hodis, Michal Harel, Joel L. Sussman, Jaime Prilusky, OCA

Personal tools