1zy5: Difference between revisions
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|PDB= 1zy5 |SIZE=350|CAPTION= <scene name='initialview01'>1zy5</scene>, resolution 2.00Å | |PDB= 1zy5 |SIZE=350|CAPTION= <scene name='initialview01'>1zy5</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span> | ||
|GENE= GCN2, AAS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= GCN2, AAS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1zy4|1ZY4]], [[1zyc|1ZYC]], [[1zyd|1ZYD]], [[1zxe|1ZXE]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zy5 OCA], [http://www.ebi.ac.uk/pdbsum/1zy5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zy5 RCSB]</span> | |||
}} | }} | ||
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[[Category: Qiu, H.]] | [[Category: Qiu, H.]] | ||
[[Category: Roll-Mecak, A.]] | [[Category: Roll-Mecak, A.]] | ||
[[Category: amino-acid starvation]] | [[Category: amino-acid starvation]] | ||
[[Category: eif2alpha kinase]] | [[Category: eif2alpha kinase]] | ||
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[[Category: translation regulator]] | [[Category: translation regulator]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:43:11 2008'' | ||
Revision as of 01:43, 31 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | , | ||||||
| Gene: | GCN2, AAS1 (Saccharomyces cerevisiae) | ||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Related: | 1ZY4, 1ZYC, 1ZYD, 1ZXE
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of eIF2alpha Protein Kinase GCN2: R794G Hyperactivating Mutant Complexed with AMPPNP.
OverviewOverview
The GCN2 protein kinase coordinates protein synthesis with levels of amino acid stores by phosphorylating eukaryotic translation initiation factor 2. The autoinhibited form of GCN2 is activated in cells starved of amino acids by binding of uncharged tRNA to a histidyl-tRNA synthetase-like domain. Replacement of Arg-794 with Gly in the PK domain (R794G) activates GCN2 independently of tRNA binding. Crystal structures of the GCN2 protein kinase domain have been determined for wild-type and R794G mutant forms in the apo state and bound to ATP/AMPPNP. These structures reveal that GCN2 autoinhibition results from stabilization of a closed conformation that restricts ATP binding. The R794G mutant shows increased flexibility in the hinge region connecting the N- and C-lobes, resulting from loss of multiple interactions involving Arg794. This conformational change is associated with intradomain movement that enhances ATP binding and hydrolysis. We propose that intramolecular interactions following tRNA binding remodel the hinge region in a manner similar to the mechanism of enzyme activation elicited by the R794G mutation.
About this StructureAbout this Structure
1ZY5 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2., Padyana AK, Qiu H, Roll-Mecak A, Hinnebusch AG, Burley SK, J Biol Chem. 2005 Aug 12;280(32):29289-99. Epub 2005 Jun 17. PMID:15964839
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