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.


5kmg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:40, 6 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<SX load='5kmg' size='340' side='right' viewer='molstar' caption='[[5kmg]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<SX load='5kmg' size='340' side='right' viewer='molstar' caption='[[5kmg]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5kmg]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KMG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KMG FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5kmg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KMG FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=POU:PELORUSIDE+A'>POU</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nrx|3nrx]], [[2nry|2nry]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=POU:PELORUSIDE+A'>POU</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5kmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kmg OCA], [https://pdbe.org/5kmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kmg RCSB], [https://www.ebi.ac.uk/pdbsum/5kmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kmg ProSAT]</span></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5kmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kmg OCA], [http://pdbe.org/5kmg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kmg RCSB], [http://www.ebi.ac.uk/pdbsum/5kmg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kmg ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/TBA1B_PIG TBA1B_PIG]] 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. [[http://www.uniprot.org/uniprot/PRC1_HUMAN PRC1_HUMAN]] Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle.<ref>PMID:9885575</ref> <ref>PMID:12082078</ref> <ref>PMID:15297875</ref> <ref>PMID:15625105</ref> <ref>PMID:16431929</ref> <ref>PMID:19468300</ref> <ref>PMID:20691902</ref> [[http://www.uniprot.org/uniprot/TBB_PIG TBB_PIG]] 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.
+
[https://www.uniprot.org/uniprot/TBA1B_PIG TBA1B_PIG] 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.
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Proteins that associate with microtubules (MTs) are crucial to generate MT arrays and establish different cellular architectures. One example is PRC1 (protein regulator of cytokinesis 1), which cross-links antiparallel MTs and is essential for the completion of mitosis and cytokinesis. Here we describe a 4-A-resolution cryo-EM structure of monomeric PRC1 bound to MTs. Residues in the spectrin domain of PRC1 contacting the MT are highly conserved and interact with the same pocket recognized by kinesin. We additionally found that PRC1 promotes MT assembly even in the presence of the MT stabilizer taxol. Interestingly, the angle of the spectrin domain on the MT surface corresponds to the previously observed cross-bridge angle between MTs cross-linked by full-length, dimeric PRC1. This finding, together with molecular dynamic simulations describing the intrinsic flexibility of PRC1, suggests that the MT-spectrin domain interface determines the geometry of the MT arrays cross-linked by PRC1.
+
-
 
+
-
Near-atomic cryo-EM structure of PRC1 bound to the microtubule.,Kellogg EH, Howes S, Ti SC, Ramirez-Aportela E, Kapoor TM, Chacon P, Nogales E Proc Natl Acad Sci U S A. 2016 Aug 23;113(34):9430-9. doi:, 10.1073/pnas.1609903113. Epub 2016 Aug 4. PMID:27493215<ref>PMID:27493215</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5kmg" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</SX>
</SX>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
-
[[Category: Chacon, P]]
+
[[Category: Chacon P]]
-
[[Category: Howes, S]]
+
[[Category: Howes S]]
-
[[Category: Kapoor, T M]]
+
[[Category: Kapoor TM]]
-
[[Category: Kellogg, E H]]
+
[[Category: Kellogg EH]]
-
[[Category: Nogales, E]]
+
[[Category: Nogales E]]
-
[[Category: Ramirez-Aportela, E]]
+
[[Category: Ramirez-Aportela E]]
-
[[Category: Ti, S C]]
+
[[Category: Ti S-C]]
-
[[Category: Cytoskeleton]]
+
-
[[Category: Microtubule]]
+
-
[[Category: Microtubule-associated protein]]
+
-
[[Category: Mitosis]]
+
-
[[Category: Structural protein]]
+

Current revision

Near-atomic cryo-EM structure of PRC1 bound to the microtubule

5kmg, resolution 3.50Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5kmg"
Personal tools