2hxh

From Proteopedia

(Difference between revisions)

Revision as of 07:01, 10 November 2021

KIF1A head-microtubule complex structure in adp-form

2hxh, resolution 11.00Å

Structural highlights

2hxh is a 3 chain structure with sequence from Lk3 transgenic mice and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1jff, 1i5s, 1ia0, 2hxf
Gene:	KIF1A (LK3 transgenic mice)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TBA1A_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. [KIF1A_MOUSE] Motor for anterograde axonal transport of synaptic vesicle precursors. [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.

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Kinesin is an ATP-driven microtubule (MT)-based motor fundamental to organelle transport. Although a number of kinesin crystal structures have been solved, the structural evidence for coupling between the bound nucleotide and the conformation of kinesin is elusive. In addition, the structural basis of the MT-induced ATPase activity of kinesin is not clear because of the absence of the MT in the structure. Here, we report cryo-electron microscopy structures of the monomeric kinesin KIF1A-MT complex in two nucleotide states at about 10 A resolution, sufficient to reveal the secondary structure. These high-resolution maps visualized clear structural changes that suggest a mechanical pathway from the nucleotide to the neck linker via the motor core rotation. In addition, new nucleotide binding pocket conformations are observed that are different from X-ray crystallographic structures; it is closed in the 5'-adenylyl-imidodiphosphate state, but open in the ADP state. These results suggest a structural model of biased diffusion movement of monomeric kinesin motor.

High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations.,Kikkawa M, Hirokawa N EMBO J. 2006 Sep 20;25(18):4187-94. Epub 2006 Aug 31. PMID:16946706^[1]

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

References

↑ Kikkawa M, Hirokawa N. High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations. EMBO J. 2006 Sep 20;25(18):4187-94. Epub 2006 Aug 31. PMID:16946706

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hxh"

@@ Line 3: / Line 3: @@
 <SX load='2hxh' size='340' side='right' viewer='molstar' caption='[[2hxh]], [[Resolution|resolution]] 11.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2hxh]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] 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=2HXH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2HXH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2hxh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] 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=2HXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HXH FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jff|1jff]], [[1i5s|1i5s]], [[1ia0|1ia0]], [[2hxf|2hxf]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jff|1jff]], [[1i5s|1i5s]], [[1ia0|1ia0]], [[2hxf|2hxf]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIF1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIF1A ([https://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://proteopedia.org/fgij/fg.htm?mol=2hxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hxh OCA], [http://pdbe.org/2hxh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hxh RCSB], [http://www.ebi.ac.uk/pdbsum/2hxh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hxh ProSAT]</span></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=2hxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hxh OCA], [https://pdbe.org/2hxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hxh RCSB], [https://www.ebi.ac.uk/pdbsum/2hxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hxh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TBA1A_PIG TBA1A_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/KIF1A_MOUSE KIF1A_MOUSE]] Motor for anterograde axonal transport of synaptic vesicle precursors. [[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/TBA1A_PIG TBA1A_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/KIF1A_MOUSE KIF1A_MOUSE]] Motor for anterograde axonal transport of synaptic vesicle precursors. [[https://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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2hxh

From Proteopedia

Revision as of 07:01, 10 November 2021

KIF1A head-microtubule complex structure in adp-form

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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