5m5c

From Proteopedia

(Difference between revisions)

Revision as of 19:03, 6 March 2020

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

5m5c, resolution 4.80Å

Structural highlights

5m5c is a 5 chain structure with sequence from Bos taurus and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	5m54, 5m50
Gene:	CAMSAP1 (HUMAN)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CAMP1_HUMAN] Probable microtubule-binding protein that plays a role in the regulation of cell morphology and cytoskeletal organization. Through interaction with spectrin may regulate neurite outgrowth.^[1] ^[2] ^[3] [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). [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]

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^[4]

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

References

↑ Baines AJ, Bignone PA, King MD, Maggs AM, Bennett PM, Pinder JC, Phillips GW. The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteins. Mol Biol Evol. 2009 Sep;26(9):2005-14. doi: 10.1093/molbev/msp115. Epub 2009 Jun , 9. PMID:19508979 doi:http://dx.doi.org/10.1093/molbev/msp115
↑ Bai SW, Herrera-Abreu MT, Rohn JL, Racine V, Tajadura V, Suryavanshi N, Bechtel S, Wiemann S, Baum B, Ridley AJ. Identification and characterization of a set of conserved and new regulators of cytoskeletal organization, cell morphology and migration. BMC Biol. 2011 Aug 11;9:54. doi: 10.1186/1741-7007-9-54. PMID:21834987 doi:10.1186/1741-7007-9-54
↑ King MD, Phillips GW, Bignone PA, Hayes NV, Pinder JC, Baines AJ. A conserved sequence in calmodulin regulated spectrin-associated protein 1 links its interaction with spectrin and calmodulin to neurite outgrowth. J Neurochem. 2014 Feb;128(3):391-402. doi: 10.1111/jnc.12462. Epub 2013 Oct 24. PMID:24117850 doi:http://dx.doi.org/10.1111/jnc.12462
↑ 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 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5m5c"

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 ==Mechanism of microtubule minus-end recognition and protection by CAMSAP proteins==
-<StructureSection load='5m5c' size='340' side='right' caption='[[5m5c]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
+<SX load='5m5c' size='340' side='right' viewer='molstar' caption='[[5m5c]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[5m5c]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M5C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M5C FirstGlance]. <br>
@@ Line 20: / Line 20: @@
 </div>
 <div class="pdbe-citations 5m5c" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Tubulin|Tubulin]]
 == References ==
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Bos taurus]]
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Akhmanova, A]]
 [[Category: Atherton, J]]

5m5c

From Proteopedia

Revision as of 19:03, 6 March 2020

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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