5m97: Difference between revisions

Latest revision as of 18:32, 1 November 2023

Structure of the Mal3 EB1-like domain

Structural highlights

5m97 is a 2 chain structure with sequence from Schizosaccharomyces pombe 972h-. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.33Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAL3_SCHPO May play a role in regulating the integrity of microtubules possibly by influencing their stability. Involved in an anchoring mechanism to maintain tea2 and tip1 at growing microtubule ends. Strongly stimulates the ATPase activity of tea2.^[1] ^[2]

Publication Abstract from PubMed

Dynamic microtubule plus ends interact with various intracellular target regions such as the cell cortex and the kinetochore. Two conserved families of microtubule plus-end tracking proteins, XMAP215/TOG and EB1, play pivotal roles in regulating microtubule dynamics. Here we study the functional interplay between fission yeast Dis1/XMAP215 and Mal3/EB1. Using an in vitro microscopy assay, we find that purified Dis1 autonomously tracks growing microtubule ends and is a bona fide microtubule polymerase. Mal3 recruits additional Dis1 to microtubule ends, explaining the synergistic enhancement of microtubule dynamicity by these proteins. A non-canonical binding motif in Dis1 mediates the interaction with Mal3. X-ray crystallography shows that this novel motif interacts in an unconventional configuration with the conserved hydrophobic cavity formed within the Mal3 C-terminal region that typically interacts with the canonical SXIP motif. Selectively perturbing the Mal3-Dis1 interaction in living cells demonstrates that it is important for accurate chromosome segregation. Whereas in some metazoans the EB1-XMAP215/TOG interaction requires an additional binding partner, fission yeast relies on a direct interaction, indicating evolutionary plasticity of this critical interaction module.

An unconventional interaction between Dis1/TOG and Mal3/EB1 promotes the fidelity of chromosome segregation.,Matsuo Y, Maurer SP, Yukawa M, Zakian S, Singleton MR, Surrey T, Toda T J Cell Sci. 2016 Nov 21. pii: jcs.197533. PMID:27872152^[3]

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

References

↑ Busch KE, Hayles J, Nurse P, Brunner D. Tea2p kinesin is involved in spatial microtubule organization by transporting tip1p on microtubules. Dev Cell. 2004 Jun;6(6):831-43. PMID:15177031 doi:https://dx.doi.org/10.1016/j.devcel.2004.05.008
↑ Browning H, Hackney DD. The EB1 homolog Mal3 stimulates the ATPase of the kinesin Tea2 by recruiting it to the microtubule. J Biol Chem. 2005 Apr 1;280(13):12299-304. Epub 2005 Jan 23. PMID:15665379 doi:https://dx.doi.org/10.1074/jbc.M413620200
↑ Matsuo Y, Maurer SP, Yukawa M, Zakian S, Singleton MR, Surrey T, Toda T. An unconventional interaction between Dis1/TOG and Mal3/EB1 promotes the fidelity of chromosome segregation. J Cell Sci. 2016 Nov 21. pii: jcs.197533. PMID:27872152 doi:https://dx.doi.org/10.1242/jcs.197533

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Busch KE, Hayles J, Nurse P, Brunner D. Tea2p kinesin is involved in spatial microtubule organization by transporting tip1p on microtubules. Dev Cell. 2004 Jun;6(6):831-43. PMID:15177031 doi:https://dx.doi.org/10.1016/j.devcel.2004.05.008

[2] Browning H, Hackney DD. The EB1 homolog Mal3 stimulates the ATPase of the kinesin Tea2 by recruiting it to the microtubule. J Biol Chem. 2005 Apr 1;280(13):12299-304. Epub 2005 Jan 23. PMID:15665379 doi:https://dx.doi.org/10.1074/jbc.M413620200

[3] Matsuo Y, Maurer SP, Yukawa M, Zakian S, Singleton MR, Surrey T, Toda T. An unconventional interaction between Dis1/TOG and Mal3/EB1 promotes the fidelity of chromosome segregation. J Cell Sci. 2016 Nov 21. pii: jcs.197533. PMID:27872152 doi:https://dx.doi.org/10.1242/jcs.197533

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
 ==Structure of the Mal3 EB1-like domain==
-<StructureSection load='5m97' size='340' side='right' caption='[[5m97]], [[Resolution|resolution]] 1.33&Aring;' scene=''>
+<StructureSection load='5m97' size='340' side='right'caption='[[5m97]], [[Resolution|resolution]] 1.33&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5m97]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M97 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5m97]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M97 FirstGlance]. <br>
-</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=5m97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m97 OCA], [http://pdbe.org/5m97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m97 RCSB], [http://www.ebi.ac.uk/pdbsum/5m97 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m97 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.33&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5m97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m97 OCA], [https://pdbe.org/5m97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m97 RCSB], [https://www.ebi.ac.uk/pdbsum/5m97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m97 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MAL3_SCHPO MAL3_SCHPO]] May play a role in regulating the integrity of microtubules possibly by influencing their stability. Involved in an anchoring mechanism to maintain tea2 and tip1 at growing microtubule ends. Strongly stimulates the ATPase activity of tea2.<ref>PMID:15177031</ref> <ref>PMID:15665379</ref>
+[https://www.uniprot.org/uniprot/MAL3_SCHPO MAL3_SCHPO] May play a role in regulating the integrity of microtubules possibly by influencing their stability. Involved in an anchoring mechanism to maintain tea2 and tip1 at growing microtubule ends. Strongly stimulates the ATPase activity of tea2.<ref>PMID:15177031</ref> <ref>PMID:15665379</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Singleton, M R]]
+[[Category: Large Structures]]
-[[Category: Zakian, S]]
+[[Category: Schizosaccharomyces pombe 972h-]]
-[[Category: Cell cycle]]
+[[Category: Singleton MR]]
-[[Category: Coiled-coil]]
+[[Category: Zakian S]]
-[[Category: Eb1 domain]]
-[[Category: Microtubule-binding]]

5m97: Difference between revisions

Latest revision as of 18:32, 1 November 2023

Structure of the Mal3 EB1-like domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools