2j0w: Difference between revisions
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|PDB= 2j0w |SIZE=350|CAPTION= <scene name='initialview01'>2j0w</scene>, resolution 2.50Å | |PDB= 2j0w |SIZE=350|CAPTION= <scene name='initialview01'>2j0w</scene>, resolution 2.50Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j0w OCA], [http://www.ebi.ac.uk/pdbsum/2j0w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j0w RCSB]</span> | |||
}} | }} | ||
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[[Category: Ren, J.]] | [[Category: Ren, J.]] | ||
[[Category: Stammers, D K.]] | [[Category: Stammers, D K.]] | ||
[[Category: act domain]] | [[Category: act domain]] | ||
[[Category: allosteric regulation]] | [[Category: allosteric regulation]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''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 03:51:30 2008'' | ||
Revision as of 00:51, 31 March 2008
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| 2j0w, resolution 2.50Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | ADP, ASP, CL, MG | ||||||||||||
| Activity: | Aspartate kinase, with EC number 2.7.2.4 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF E. COLI ASPARTOKINASE III IN COMPLEX WITH ASPARTATE AND ADP (R-STATE)
Overview
Aspartokinase III (AKIII) from Escherichia coli catalyzes an initial commitment step of the aspartate pathway, giving biosynthesis of certain amino acids including lysine. We report crystal structures of AKIII in the inactive T-state with bound feedback allosteric inhibitor lysine and in the R-state with aspartate and ADP. The structures reveal an unusual configuration for the regulatory ACT domains, in which ACT2 is inserted into ACT1 rather than the expected tandem repeat. Comparison of R- and T-state AKIII indicates that binding of lysine to the regulatory ACT1 domain in R-state AKIII instigates a series of changes that release a "latch", the beta15-alphaK loop, from the catalytic domain, which in turn undergoes large rotational rearrangements, promoting tetramer formation and completion of the transition to the T-state. Lysine-induced allosteric transition in AKIII involves both destabilizing the R-state and stabilizing the T-state tetramer. Rearrangement of the catalytic domain blocks the ATP-binding site, which is therefore the structural basis for allosteric inhibition of AKIII by lysine.
About this Structure
2J0W is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine., Kotaka M, Ren J, Lockyer M, Hawkins AR, Stammers DK, J Biol Chem. 2006 Oct 20;281(42):31544-52. Epub 2006 Aug 12. PMID:16905770
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