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Catalytic Site Atlas Search Results
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UNIPROT ID
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Catalytic Site Atlas

CSA LITERATURE entry for 1goj

E.C. nameplus-end-directed kinesin ATPase
SpeciesNeurospora crassa ()
E.C. Number (IntEnz) 3.6.4.4
CSA Homologues of 1gojThere are 76 Homologs
CSA Entries With UniProtID
CSA Entries With EC Number 3.6.4.4
PDBe Entry 1goj
PDBSum Entry 1goj
MACiE Entry 1goj

Literature Report

IntroductionThe fast kinesin from the fungus N.crassa is able to use the energy from ATP hydrolysis in order to power conformational change that leads to the extension of microtubules. Its main function is to cause the growth of hyphae, the root-like system that allows the fungus to feed. Structurally the protein shows a similar catalytic domain to many other proteins involved in nucleotide hydrolysis, especially G proteins such as Ras, suggesting a common evolutionary origin. The kinesin is the fastest yet known able to cause movement of 0.5 micrometers per second.
MechansimThe reaction proceeds through in-line nucleophilic attack of a water molecule on the gamma phosphate of ATP. This results in a pentavalent phosphate transition state stabilised by contacts with the amide group of Gly 238 and the Magnesium ion at the active site. The pentavalent phosphate transition state then collapses to release ADP and Pi, resulting in the conformational change that powers the extension of the microtubules.
Reaction

Catalytic Sites for 1goj

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GlyA238238macie:mainChainAmideActs to stabilise the pentavalent phosphate transition state by neutralising the increased negative charge that builds up on the gamma phosphate.

Literature References

Notes:
Song YH
Structure of a fast kinesin: implications for ATPase mechanism and interactions with microtubules.
EMBO J 2001 20 6213-6225
PubMed: 11707393
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