From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:3cnz.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:3cnz.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_3cnz| PDB=3cnz | SCENE= }} | | {{STRUCTURE_3cnz| PDB=3cnz | SCENE= }} |
| | | | |
| - | '''Structural dynamics of the microtubule binding and regulatory elements in the kinesin-like calmodulin binding protein'''
| + | ===Structural dynamics of the microtubule binding and regulatory elements in the kinesin-like calmodulin binding protein=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Kinesins are molecular motors that power cell division and transport of various proteins and organelles. Their motor activity is driven by ATP hydrolysis and depends on interactions with microtubule tracks. Essential steps in kinesin movement rely on controlled alternate binding to and detaching from the microtubules. The conformational changes in the kinesin motors induced by nucleotide and microtubule binding are coordinated by structural elements within their motor domains. Loop L11 of the kinesin motor domain interacts with the microtubule and is implicated in both microtubule binding and sensing nucleotide bound to the active site of kinesin. Consistent with its proposed role as a microtubule sensor, loop L11 is rarely seen in crystal structures of unattached kinesins. Here, we report four structures of a regulated plant kinesin, the kinesin-like calmodulin binding protein (KCBP), determined by X-ray crystallography. Although all structures reveal the kinesin motor in the ATP-like conformation, its loop L11 is observed in different conformational states, both ordered and disordered. When structured, loop L11 adds three additional helical turns to the N-terminal part of the following helix alpha4. Although interactions with protein neighbors in the crystal support the ordering of loop L11, its observed conformation suggests the conformation for loop L11 in the microtubule-bound kinesin. Variations in the positions of other features of these kinesins were observed. A critical regulatory element of this kinesin, the calmodulin binding helix positioned at the C-terminus of the motor domain, is thought to confer negative regulation of KCBP. Calmodulin binds to this helix and inserts itself between the motor and the microtubule. Comparison of five independent structures of KCBP shows that the positioning of the calmodulin binding helix is not decided by crystal packing forces but is determined by the conformational state of the motor. The observed variations in the position of the calmodulin binding helix fit the regulatory mechanism previously proposed for this kinesin motor.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18513992}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18513992 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_18513992}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 35: |
Line 39: |
| | [[Category: Nucleotide-binding]] | | [[Category: Nucleotide-binding]] |
| | [[Category: Switch ii]] | | [[Category: Switch ii]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:10:58 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 16 08:54:00 2008'' |
Revision as of 05:54, 16 July 2008
Template:STRUCTURE 3cnz
Structural dynamics of the microtubule binding and regulatory elements in the kinesin-like calmodulin binding protein
Template:ABSTRACT PUBMED 18513992
About this Structure
3CNZ is a Single protein structure of sequence from Solanum tuberosum. Full crystallographic information is available from OCA.
Reference
Structural dynamics of the microtubule binding and regulatory elements in the kinesin-like calmodulin binding protein., Vinogradova MV, Malanina GG, Reddy VS, Reddy AS, Fletterick RJ, J Struct Biol. 2008 May 5;. PMID:18513992
Page seeded by OCA on Wed Jul 16 08:54:00 2008
