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.

1goj

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 11:26, 28 July 2021

Structure of a fast kinesin: Implications for ATPase mechanism and interactions with microtubules

Structural highlights

1goj is a 1 chain structure with sequence from Chrysonilia crassa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Plus-end-directed kinesin ATPase, with EC number 3.6.4.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KINH_NEUCR] Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Its motor activity is directed toward the microtubule's plus end.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We determined the crystal structure of the motor domain of the fast fungal kinesin from Neurospora crassa (NcKin). The structure has several unique features. (i) Loop 11 in the switch 2 region is ordered and enables one to describe the complete nucleotide-binding pocket, including three inter-switch salt bridges between switch 1 and 2. (ii) Loop 9 in the switch 1 region bends outwards, making the nucleotide-binding pocket very wide. The displacement in switch 1 resembles that of the G-protein ras complexed with its guanosine nucleotide exchange factor. (iii) Loop 5 in the entrance to the nucleotide-binding pocket is remarkably long and interacts with the ribose of ATP. (iv) The linker and neck region is not well defined, indicating that it is mobile. (v) Image reconstructions of ice-embedded microtubules decorated with NcKin show that it interacts with several tubulin subunits, including a central beta-tubulin monomer and the two flanking alpha-tubulin monomers within the microtubule protofilament. Comparison of NcKin with other kinesins, myosin and G-proteins suggests that the rate-limiting step of ADP release is accelerated in the fungal kinesin and accounts for the unusually high velocity and ATPase activity.

Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules.,Song YH, Marx A, Muller J, Woehlke G, Schliwa M, Krebs A, Hoenger A, Mandelkow E EMBO J. 2001 Nov 15;20(22):6213-25. PMID:11707393^[1]

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

References

↑ Song YH, Marx A, Muller J, Woehlke G, Schliwa M, Krebs A, Hoenger A, Mandelkow E. Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules. EMBO J. 2001 Nov 15;20(22):6213-25. PMID:11707393 doi:10.1093/emboj/20.22.6213

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/1goj"

@@ Line 3: / Line 3: @@
 <StructureSection load='1goj' size='340' side='right'caption='[[1goj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1goj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GOJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1goj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GOJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Plus-end-directed_kinesin_ATPase Plus-end-directed kinesin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.4 3.6.4.4] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Plus-end-directed_kinesin_ATPase Plus-end-directed kinesin ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.4 3.6.4.4] </span></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=1goj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1goj OCA], [http://pdbe.org/1goj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1goj RCSB], [http://www.ebi.ac.uk/pdbsum/1goj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1goj 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=1goj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1goj OCA], [https://pdbe.org/1goj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1goj RCSB], [https://www.ebi.ac.uk/pdbsum/1goj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1goj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KINH_NEUCR KINH_NEUCR]] Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Its motor activity is directed toward the microtubule's plus end.
+[[https://www.uniprot.org/uniprot/KINH_NEUCR KINH_NEUCR]] Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Its motor activity is directed toward the microtubule's plus end.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1goj

From Proteopedia

Revision as of 11:26, 28 July 2021

Structure of a fast kinesin: Implications for ATPase mechanism and interactions with microtubules

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox