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.

5m50

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:10, 15 November 2017

Mechanism of microtubule minus-end recognition and protection by CAMSAP proteins

Structural highlights

5m50 is a 5 chain structure with sequence from Bos taurus and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Gene:	Camsap3, Kiaa1543 (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[F2Z4C1_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.[RuleBase:RU000352][SAAS:SAAS00824325] [CAMP3_MOUSE] Microtubule minus-end binding protein that acts as a regulator of microtubule dynamics. Specifically required for zonula adherens biogenesis and maintenance by anchoring microtubules at their minus-ends to zonula adherens, leading to recruit KIFC3 kinesin to junctional site (By similarity). [TBB2B_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).

Publication Abstract from PubMed

CAMSAP and Patronin family members regulate microtubule minus-end stability and localization and thus organize noncentrosomal microtubule networks, which are essential for cell division, polarization and differentiation. Here, we found that the CAMSAP C-terminal CKK domain is widely present among eukaryotes and autonomously recognizes microtubule minus ends. Through a combination of structural approaches, we uncovered how mammalian CKK binds between two tubulin dimers at the interprotofilament interface on the outer microtubule surface. In vitro reconstitution assays combined with high-resolution fluorescence microscopy and cryo-electron tomography suggested that CKK preferentially associates with the transition zone between curved protofilaments and the regular microtubule lattice. We propose that minus-end-specific features of the interprotofilament interface at this site serve as the basis for CKK's minus-end preference. The steric clash between microtubule-bound CKK and kinesin motors explains how CKK protects microtubule minus ends against kinesin-13-induced depolymerization and thus controls the stability of free microtubule minus ends.

A structural model for microtubule minus-end recognition and protection by CAMSAP proteins.,Atherton J, Jiang K, Stangier MM, Luo Y, Hua S, Houben K, van Hooff JJE, Joseph AP, Scarabelli G, Grant BJ, Roberts AJ, Topf M, Steinmetz MO, Baldus M, Moores CA, Akhmanova A Nat Struct Mol Biol. 2017 Oct 9. doi: 10.1038/nsmb.3483. PMID:28991265^[1]

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

References

↑ Atherton J, Jiang K, Stangier MM, Luo Y, Hua S, Houben K, van Hooff JJE, Joseph AP, Scarabelli G, Grant BJ, Roberts AJ, Topf M, Steinmetz MO, Baldus M, Moores CA, Akhmanova A. A structural model for microtubule minus-end recognition and protection by CAMSAP proteins. Nat Struct Mol Biol. 2017 Oct 9. doi: 10.1038/nsmb.3483. PMID:28991265 doi:http://dx.doi.org/10.1038/nsmb.3483

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/5m50"

@@ Line 3: / Line 3: @@
 <StructureSection load='5m50' size='340' side='right' caption='[[5m50]], [[Resolution|resolution]] 5.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5m50]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M50 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M50 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5m50]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M50 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M50 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Camsap3, Kiaa1543 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5m50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m50 OCA], [http://pdbe.org/5m50 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m50 RCSB], [http://www.ebi.ac.uk/pdbsum/5m50 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m50 ProSAT]</span></td></tr>
 </table>
@@ Line 23: / Line 24: @@
 </StructureSection>
 [[Category: Bos taurus]]
+[[Category: Lk3 transgenic mice]]
 [[Category: Akhmanova, A]]
 [[Category: Atherton, J]]

5m50

From Proteopedia

Revision as of 10:10, 15 November 2017

Mechanism of microtubule minus-end recognition and protection by CAMSAP proteins

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox