5ve9

From Proteopedia

(Difference between revisions)

Revision as of 10:37, 13 September 2017

Structure of hACF7 EF1-EF2-GAR domains

Structural highlights

5ve9 is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MACF1_HUMAN] Isoform 2 is a F-actin-binding protein which may play a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane. Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics. May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4. Plays a key role in wound healing and epidermal cell migration. Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate MT dynamics and polarize hair follicle stem cells (By similarity).^[1] ^[2]

Publication Abstract from PubMed

Spectraplakins are large molecules that cross-link F-actin and microtubules (MTs). Mutations in spectraplakins yield defective cell polarization, aberrant focal adhesion dynamics, and dystonia. We present the 2.8 A crystal structure of the hACF7 EF1-EF2-GAR MT-binding module and delineate the GAR residues critical for MT binding. The EF1-EF2 and GAR domains are autonomous domains connected by a flexible linker. The EF1-EF2 domain is an EFbeta-scaffold with two bound Ca2+ ions that straddle an N-terminal alpha helix. The GAR domain has a unique alpha/beta sandwich fold that coordinates Zn2+. While the EF1-EF2 domain is not sufficient for MT binding, the GAR domain is and likely enhances EF1-EF2-MT engagement. Residues in a conserved basic patch, distal to the GAR domain's Zn2+-binding site, mediate MT binding.

Structure of the ACF7 EF-Hand-GAR Module and Delineation of Microtubule Binding Determinants.,Lane TR, Fuchs E, Slep KC Structure. 2017 Jul 5;25(7):1130-1138.e6. doi: 10.1016/j.str.2017.05.006. Epub, 2017 Jun 8. PMID:28602822^[3]

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

References

↑ Kakinuma T, Ichikawa H, Tsukada Y, Nakamura T, Toh BH. Interaction between p230 and MACF1 is associated with transport of a glycosyl phosphatidyl inositol-anchored protein from the Golgi to the cell periphery. Exp Cell Res. 2004 Aug 15;298(2):388-98. PMID:15265687 doi:http://dx.doi.org/10.1016/j.yexcr.2004.04.047
↑ Zaoui K, Benseddik K, Daou P, Salaun D, Badache A. ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells. Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18517-22. doi:, 10.1073/pnas.1000975107. Epub 2010 Oct 11. PMID:20937854 doi:10.1073/pnas.1000975107
↑ Lane TR, Fuchs E, Slep KC. Structure of the ACF7 EF-Hand-GAR Module and Delineation of Microtubule Binding Determinants. Structure. 2017 Jul 5;25(7):1130-1138.e6. doi: 10.1016/j.str.2017.05.006. Epub, 2017 Jun 8. PMID:28602822 doi:http://dx.doi.org/10.1016/j.str.2017.05.006

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ve9"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5ve9 is ON HOLD
+==Structure of hACF7 EF1-EF2-GAR domains==
+<StructureSection load='5ve9' size='340' side='right' caption='[[5ve9]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ve9]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VE9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VE9 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ve9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ve9 OCA], [http://pdbe.org/5ve9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ve9 RCSB], [http://www.ebi.ac.uk/pdbsum/5ve9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ve9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MACF1_HUMAN MACF1_HUMAN]] Isoform 2 is a F-actin-binding protein which may play a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane. Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics. May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4. Plays a key role in wound healing and epidermal cell migration. Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate MT dynamics and polarize hair follicle stem cells (By similarity).<ref>PMID:15265687</ref> <ref>PMID:20937854</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Spectraplakins are large molecules that cross-link F-actin and microtubules (MTs). Mutations in spectraplakins yield defective cell polarization, aberrant focal adhesion dynamics, and dystonia. We present the 2.8 A crystal structure of the hACF7 EF1-EF2-GAR MT-binding module and delineate the GAR residues critical for MT binding. The EF1-EF2 and GAR domains are autonomous domains connected by a flexible linker. The EF1-EF2 domain is an EFbeta-scaffold with two bound Ca2+ ions that straddle an N-terminal alpha helix. The GAR domain has a unique alpha/beta sandwich fold that coordinates Zn2+. While the EF1-EF2 domain is not sufficient for MT binding, the GAR domain is and likely enhances EF1-EF2-MT engagement. Residues in a conserved basic patch, distal to the GAR domain's Zn2+-binding site, mediate MT binding.
-Authors:
+Structure of the ACF7 EF-Hand-GAR Module and Delineation of Microtubule Binding Determinants.,Lane TR, Fuchs E, Slep KC Structure. 2017 Jul 5;25(7):1130-1138.e6. doi: 10.1016/j.str.2017.05.006. Epub, 2017 Jun 8. PMID:28602822<ref>PMID:28602822</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5ve9" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Lane, T R]]
+[[Category: Slep, K C]]
+[[Category: Ef-hand]]
+[[Category: Gas2]]
+[[Category: Microtubule binding]]
+[[Category: Protein binding]]
+[[Category: Spectraplakin]]

5ve9

From Proteopedia

Revision as of 10:37, 13 September 2017

Structure of hACF7 EF1-EF2-GAR domains

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox