User:Natalya Boufan/Sandbox 1

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The AceK structure contains two functional domains: a Kinase domain (KD) where the kinase, phosphatase and ATPase reactions occur, and a regulatory (RD) that helps form allosteric binding pockets involved in regulating the catalytic domain’s function. The <scene name='78/783138/Amp_binding/7'>AMP molecule</scene> is situated in a pocket at the interface between the KD and RD and acts as a bridge.
The AceK structure contains two functional domains: a Kinase domain (KD) where the kinase, phosphatase and ATPase reactions occur, and a regulatory (RD) that helps form allosteric binding pockets involved in regulating the catalytic domain’s function. The <scene name='78/783138/Amp_binding/7'>AMP molecule</scene> is situated in a pocket at the interface between the KD and RD and acts as a bridge.
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The <scene name='78/783138/Regulation_domain/4'>regulatory domain</scene>, which comprises the amino-terminal half of the AceK sequence, is mainly composed of a-helices. It begins with two long, parallel a-helices that form a large hairpin structure, followed by two short, parallel a-helices that form a small hairpin segment. The regulatory domain is linked to the kinase domain by a 27-residue-long a-helix. This domain represents a unique protein fold with no structural homologues.
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The <scene name='78/783138/Regulation_domain/4'>regulatory domain</scene>, which comprises the amino-terminal half of the AceK sequence, is mainly composed of a-helices and hairpin structures.This domain represents a unique protein fold with no structural homologues. The regulatory domain is linked to the kinase domain by a 27-residue-long a-helix. The <scene name='78/783138/Kinase_domain/13'>kinase domain</scene>, which makes up the carboxy-terminal half of AceK, has a classic bi-lobe protein kinase fold with the <scene name='78/783138/Atp_binding_site/1'>ATP-binding cleft</scene> located at the interface between the two lobes. The N-terminal lobe consists mainly of a twisted, five-stranded, antiparallel b-sheet and two a-helices. The larger C-terminal lobe is predominantly a-helical with some stretches of antiparallel b-strands. The ATP molecule is under the cover of the five-stranded b-sheet and is shielded by <scene name='78/783138/Loopb/3'>loop-b3aC</scene>. Loop-b3aC shifts upwards or downwards to controls access to the ATP-binding site. The <scene name='78/783138/Srl/1'>substrate recognition loop</scene> (SRL) stretches out of the C-terminal lobe. This loop, together with loop-b3aC, forms a large cleft that is the <scene name='78/783138/Icdh_binding_cleft/1'>IDH binding site</scene>.
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The <scene name='78/783138/Kinase_domain/13'>kinase domain</scene>, which makes up the carboxy-terminal half of AceK, has a classic bi-lobe protein kinase fold with the <scene name='78/783138/Atp_binding_site/1'>ATP-binding cleft</scene> located at the interface between the two lobes. The N-terminal lobe consists mainly of a twisted, five-stranded, antiparallel b-sheet and two a-helices. The larger C-terminal lobe is predominantly a-helical with some stretches of antiparallel b-strands. The ATP molecule is under the cover of the five-stranded b-sheet and is shielded by <scene name='78/783138/Loopb/3'>loop-b3aC</scene>. Loop-b3aC shifts upwards or downwards to controls access to the ATP-binding site. The <scene name='78/783138/Srl/1'>substrate recognition loop</scene> (SRL) stretches out of the C-terminal lobe. This loop, together with loop-b3aC, forms a large cleft that is the <scene name='78/783138/Icdh_binding_cleft/1'>IDH binding site</scene>.
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= Function =
= Function =

Revision as of 15:16, 19 March 2018

Isocitrate dehydrogenase kinase/phosphatase

The AMP-bound AceK structure

Drag the structure with the mouse to rotate

References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)

Natalya Boufan

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